ApoList – January 2020


Immunogenicity of cell death


Quantitative and Dynamic Catalogs of Proteins Released during Apoptotic and Necroptotic Cell Death – Maria C. Tanzer, Annika Frauenstein, Che A. Stafford, Kshiti Phulphagar, Matthias Mann, Felix Meissner. https://www.cell.com/cell-reports/fulltext/S2211-1247(19)31744-9

Immunodominant AH1 Antigen-Deficient Necroptotic, but Not Apoptotic, Murine Cancer Cells Induce Antitumor Protection – Tania Løve Aaes, Hanne Verschuere, Agnieszka Kaczmarek, Liesbeth Heyndrickx, Bartosz Wiernicki, Iris Delrue, Bram De Craene, Joachim Taminau, Tinneke Delvaeye, Mathieu J. M. Bertrand, Wim Declercq, Geert Berx, Dmitri V. Krysko, Sandy Adjemian and Peter Vandenabeele. https://www.jimmunol.org/content/early/2020/01/02/jimmunol.1900072

Immune Sensing of Cell Death through Recognition of Histone Sequences by C-Type Lectin-Receptor-2d Causes Inflammation and Tissue Injury – Jiann-Jyh Lai, Freidrich M. Cruz, Kenneth L. Rock. https://www.cell.com/immunity/fulltext/S1074-7613(19)30494-7

Characterization of virus-mediated immunogenic cancer cell death and the consequences for oncolytic virus-based immunotherapy of cancer – Jing Ma, Mohanraj Ramachandran, Chuan Jin, Clara Quijano-Rubio, Miika Martikainen, Di Yu and Magnus Essand. https://www.nature.com/articles/s41419-020-2236-3


Death receptors


Misfolded proteins bind and activate death receptor 5 to induce apoptosis during unresolved endoplasmic reticulum stress – Mable Lam, Scot A Marsters, Avi Ashkenazi, Peter Walter. https://elifesciences.org/articles/52291

Heterogeneous responses to low level death receptor activation are explained by random molecular assembly of the Caspase-8 activation platform – Matveeva A, Fichtner M, McAllister K, McCann C, Sturrock M, Longley DB, Prehn JHM. https://journals.plos.org/ploscompbiol/article?id=10.1371/journal.pcbi.1007374

Single-molecule imaging reveals the oligomeric state of functional TNFα-induced plasma membrane TNFR1 clusters in cells – Christos Karathanasis, Juliane Medler, Franziska Fricke, Sonja Smith, Sebastian Malkusch, Darius Widera, Simone Fulda, Harald Wajant, Sjoerd J. L. van Wijk, Ivan Dikic and Mike Heilemann. https://stke.sciencemag.org/content/13/614/eaax5647


Bcl-2 family proteins


Mitochondrial residence of the apoptosis inducer BAX is more important than BAX oligomerization in promoting membrane permeabilization – Tomomi Kuwana, Louise E King, Katia Cosentino, Julian Suess, Ana J. García-Sáez, Andrew P. Gilmore and Donald D Newmeyer. http://www.jbc.org/content/early/2020/01/03/jbc.RA119.011635.abstract

Dynein light chain binding determines complex formation and posttranslational stability of the Bcl-2 family members Bmf and Bim – Prafull Kumar Singh, Aristomenis Roukounakis, Arnim Weber, Kushal Kumar Das, Benedicte Sohm, Andreas Villunger, Ana J. Garcia-Saez and Georg Häcker. https://www.nature.com/articles/s41418-019-0365-y

Loss of Bcl-G, a Bcl-2 family member, augments the development of inflammation-associated colorectal cancer – Paul M. Nguyen, Laura F. Dagley, Adele Preaudet, Nga Lam, Maybelline Giam, Ka Yee Fung, Kaheina Aizel, Gemma van Duijneveldt, Chin Wee Tan, Yumiko Hirokawa, Hon Yan K. Yip, Christopher G. Love, Ashleigh R. Poh, Akshay D’ Cruz, Charlotte Burstroem, Rebecca Feltham, Suad M. Abdirahman, Kristy Meiselbach, Ronnie Ren Jie Low, Michelle Palmieri, Matthias Ernst, Andrew I. Webb, Tony Burgess, Oliver M. Sieber, Philippe Bouillet and Tracy L. Putoczki. https://www.nature.com/articles/s41418-019-0383-9

Human BCL-G regulates secretion of inflammatory chemokines but is dispensable for induction of apoptosis by IFN-γ and TNF-α in intestinal epithelial cells – Jerzy A. Woznicki, Peter Flood, Milan Bustamante-Garrido, Panagiota Stamou, Gerry Moloney, Aine Fanning, Syed Akbar Zulquernain, Jane McCarthy, Fergus Shanahan, Silvia Melgar and Ken Nally. https://www.nature.com/articles/s41419-020-2263-0

Characterization of a novel human BFL-1-specific monoclonal antibody – Lahiru Gangoda, Charis E. Teh, Michael A. Dengler, Sarah A. Best, Clare E. Weeden, Lin Tai, Erinna F. Lee, Walter D. Fairlie, Kate D. Sutherland, Leonard C. Harrison, Daniel H. Gray, Andreas Strasser and Marco J. Herold. https://www.nature.com/articles/s41418-019-0454-y

Bile acid-induced “Minority MOMP” promotes esophageal carcinogenesis while maintaining apoptotic resistance via Mcl-1 – Yuan Xu, Deborah R. Surman, Laurence Diggs, Sichuan Xi, Shaojian Gao, Devikala Gurusamy, Kaitlin McLoughlin, Justin Drake, Paul Feingold, Kate Brown, Danny Wangsa, Darawalee Wangsa, Xi Zhang, Thomas Ried, Jeremy L. Davis, Jonathan Hernandez, Chuong D. Hoang, Rhonda F. Souza, David S. Schrump and R. Taylor Ripley. https://www.nature.com/articles/s41388-019-1029-6

The carboxyl-terminal sequence of bim enables bax activation and killing of unprimed cells – Xiaoke Chi, Dang Nguyen, James M Pemberton, Elizabeth J Oesterlund, Qian Liu, Hetal Brahmbhatt, Zhi Zhang, Jialing Lin, Brian Leber, David W Andrews. https://elifesciences.org/articles/44525

Type 1 Innate Lymphoid Cells Protect Mice from Acute Liver Injury via Interferon-γ Secretion for Upregulating Bcl-xL Expression in Hepatocytes – Tsukasa Nabekura, Luke Riggan, Andrew D. Hildreth, Timothy E. O’Sullivan, Akira Shibuya. https://www.cell.com/immunity/fulltext/S1074-7613(19)30462-5


Caspases


Exploring the prime site in caspases as a novel chemical strategy for understanding the mechanisms of cell death: a proof of concept study on necroptosis in cancer cells – Katarzyna Groborz, Monica L. Gonzalez Ramirez, Scott J. Snipas, Guy S. Salvesen, Marcin Drąg and Marcin Poręba. https://www.nature.com/articles/s41418-019-0364-z


Necroptosis / RIP kinases


CK1α, CK1δ, and CK1ε are necrosome components which phosphorylate serine 227 of human RIPK3 to activate necroptosis – Sarah Hanna-Addams, Shuzhen Liu, Hua Liu, She Chen and Zhigao Wang. https://www.pnas.org/content/117/4/1962.abstract?etoc

Casein kinase-1γ1 and 3 stimulate tumor necrosis factor-induced necroptosis through RIPK3 – Song-Yi Lee, Hyunjoo Kim, Cathena Meiling Li, Jaemin Kang, Ayaz Najafov, Muhah Jung, Soosung Kang, Shaomeng Wang, Junying Yuan and Yong-Keun Jung. https://www.nature.com/articles/s41419-019-2146-4

Constitutive Interferon Attenuates RIPK1/3-Mediated Cytokine Translation – Hayley I. Muendlein, Joseph Sarhan, Beiyun C. Liu, Wilson M. Connolly, Stephen A. Schworer, Irina Smirnova, Amy Y. Tang, Vladimir Ilyukha, Jodie Pietruska, Soroush Tahmasebi, Nahum Sonenberg, Alexei Degterev, Alexander Poltorak. https://www.cell.com/cell-reports/fulltext/S2211-1247(19)31730-9

Resolvin D1 promotes the targeting and clearance of necroptotic cells – Brennan D. Gerlach, Michael Marinello, Justin Heinz, Nicholas Rymut, Brian E. Sansbury, Colin O. Riley, Sudeshna Sadhu, Zeinab Hosseini, Yoko Kojima, Dale D. Tang, Nicholas J. Leeper, Matthew Spite, Margarida Barroso, Katey J. Rayner and Gabrielle Fredman. https://www.nature.com/articles/s41418-019-0370-1


Ferroptosis


ATF3 promotes erastin-induced ferroptosis by suppressing system Xc – Liyuan Wang, Yichen Liu, Tingting Du, Heng Yang, Lei Lei, Mengqi Guo, Han-Fei Ding, Junran Zhang, Hongbo Wang, Xiaoguang Chen and Chunhong Yan. https://www.nature.com/articles/s41418-019-0380-z


Miscellanous


Programmed cell death along the midline axis patterns ipsilaterality in gastrulation – Lisandro Maya-Ramos, Takashi Mikawa. https://science.sciencemag.org/content/367/6474/197

Nuclear degradation dynamics in a nonapoptotic programmed cell death – Alla Yalonetskaya, Albert A. Mondragon, Zackary J. Hintze, Susan Holmes and Kimberly McCall. https://www.nature.com/articles/s41418-019-0382-x


Reviews


Mitochondria as multifaceted regulators of cell death – Florian J. Bock and Stephen W. G. Tait. https://www.nature.com/articles/s41580-019-0173-8

Beyond inflammasomes: emerging function of gasdermins during apoptosis and NETosis – Kaiwen W Chen, Benjamin Demarco, Petr Broz. https://www.embopress.org/doi/abs/10.15252/embj.2019103397

Immunological impact of cell death signaling driven by radiation on the tumor microenvironment – Maria Esperanza Rodriguez-Ruiz, Ilio Vitale, Kevin J. Harrington, Ignacio Melero and Lorenzo Galluzzi. https://www.nature.com/articles/s41590-019-0561-4

Saga of Mcl-1: regulation from transcription to degradation – Viacheslav V. Senichkin, Alena Y. Streletskaia, Anna S. Gorbunova, Boris Zhivotovsky and Gelina S. Kopeina. https://www.nature.com/articles/s41418-019-0486-3


Comments


A matter of life and death for caspase 8 – Joseph Willson. https://www.nature.com/articles/s41580-019-0201-8

Clec2d Joins the Cell Death Sensor Ranks – Carlos del Fresno, David Sancho. https://www.cell.com/immunity/fulltext/S1074-7613(19)30534-5

 

Apolist – April 2011

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Bcl-2 family members
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Discovery and molecular characterization of a Bcl-2–regulated cell death pathway in schistosomes
Erinna F. Lee, Oliver B. Clarke, Marco Evangelista, Zhiping Feng, Terence P. Speed, Elissaveta B. Tchoubrieva, Andreas Strasser, Bernd H. Kalinna, Peter M. Colman, and W. Douglas Fairlie
http://www.pnas.org/content/108/17/6999.abstract?etoc

Selective involvement of BH3-only proteins and differential targets of Noxa in diverse apoptotic pathways
L Zhang, H Lopez, N M George, X Liu, X Pang and X Luo
http://www.nature.com/cdd/journal/v18/n5/full/cdd2010152a.html

Investigation of the Bcl-2 multimerisation process: Structural and functional implications
Alessia, Camperchioli | Marisa, Mariani | Silvia, Bartollino | Lella, Petrella | Marco, Persico | Nausicaa, Orteca | Giovanni, Scambia | Shohreh, Shahabi | Cristiano, Ferlini | Caterina, Fattorusso
http://dx.doi.org/10.1016/j.bbamcr.2011.02.006

Bcl-xL Retrotranslocates Bax from the Mitochondria into the Cytosol
F. Edlich, S. Banerjee, M. Suzuki, M.M. Cleland, D. Arnoult, C. Wang, A. Neutzner, N. Tjandra, and R.J. Youle
http://www.cell.com/abstract/S0092-8674%2811%2900186-3

Mitochondrial BCL-2 inhibits AMBRA1-induced autophagy
FlavieStrappazzon, Matteo Vietri-Rudan, Silvia Campello, Francesca Nazio, Fulvio Florenzano, Gian Maria Fimia, Mauro Piacentini, Beth Levine and Francesco Cecconi
http://www.nature.com/emboj/journal/v30/n7/abs/emboj201149a.html

Arginine methylation of BCL-2 antagonist of cell death (BAD) counteracts its phosphorylation and inactivation by Akt
Jun-ichi Sakamaki, Hiroaki Daitoku, Katsuya Ueno, Ayano Hagiwara, Kazuyuki Yamagata, and Akiyoshi Fukamizu
http://www.pnas.org/content/108/15/6085.abstract?etoc

Mcl-1 is critical for survival in a subgroup of non-small-cell lung cancer cell lines
H Zhang, S Guttikonda, L Roberts, T Uziel, D Semizarov, S W Elmore, J D Leverson and L T Lam
http://www.nature.com/onc/journal/v30/n16/full/onc2010559a.html

The Anti-Apoptotic Bcl-xL Protein, a New Piece in the Puzzle of Cytochrome C Interactome
Ivano Bertini, Soizic Chevance, Rebecca Del Conte, Daniela Lalli, Paola Turano
http://www.plosone.org/article/info:doi/10.1371/journal.pone.0018329

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Death receptors and IAPs
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NEMO and RIP1 Control Cell Fate in Response to Extensive DNA Damage via TNF-α Feedforward Signaling
S. Biton and A. Ashkenazi
http://www.cell.com/abstract/S0092-8674%2811%2900175-9

UXT-V1 protects cells against TNF-induced apoptosis through modulating complex II formation
Yuefeng Huang, Liang Chen, Yi Zhou, Heng Liu, Jueqing Yang, Zhenggang Liu, and Chen Wang
http://www.molbiolcell.org/cgi/content/abstract/22/8/1389?etoc

Deletion of cIAP1 and cIAP2 in murine B lymphocytes constitutively activates cell survival pathways and inactivates the germinal center response
Sandra Gardam, Vivian M. Turner, Holly Anderton, Sandhya Limaye, Antony Basten, Frank Koentgen, David L. Vaux, John Silke, and Robert Brink
http://bloodjournal.hematologylibrary.org/cgi/content/abstract/117/15/4041

TWEAK induces apoptosis through a death-signaling complex comprising receptor-interacting protein 1 (RIP1), Fas-associated death domain (FADD) and caspase-8
Aminah Ikner and Avi Ashkenazi
http://www.jbc.org/cgi/content/abstract/M110.203745v1

Characterization of dequalinium as a XIAP antagonist that targets the BIR2 domain
Mar Orzáez, Anna Gortat, Mónica Sancho, Rodrigo J. Carbajo, Antonio Pineda-Lucena, Yadira Palacios-Rodríguez & Enrique Pérez-Payá
http://www.springerlink.com/content/xm45135052573643/

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Caspases and execution phase
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Concerted antigen processing of a short viral antigen by human caspases 5 and 10
Daniel López, Mercedes Jiménez, Margarita Garcia-Calvo, and Margarita Del Val
J. Biol. Chem. published 28 March 2011, 10.1074/jbc.M111.234658
http://www.jbc.org/cgi/content/abstract/M111.234658v1

Apoptotic microtubule network organization and maintenance depend on high cellular ATP levels and energized mitochondria
Manuel Oropesa, Mario de la Mata, Juan Garrido Maraver, Mario D. Cordero, David Cotán, Ángeles Rodríguez-Hernández, Irene Domínguez-Moñino, Manuel de Miguel, Plácido Navas & José A. Sánchez-Alcázar
http://www.springerlink.com/content/47h1021vl35l1h77/

Receptor for advanced glycation end products binds to phosphatidylserine and assists in the clearance of apoptotic cells
Mei He, Hiroshi Kubo, Konosuke Morimoto, Naoya Fujino, Takaya Suzuki, Toru Takahasi, Mitsuhiro Yamada, Mutsuo Yamaya, Tomoyuki Maekawa, Yasuhiko Yamamoto and Hiroshi Yamamoto
http://www.nature.com/embor/journal/v12/n4/full/embor201128a.html

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MISCELLANEOUS
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Mechanisms of necroptosis in T cells
Irene L. Ch’en, Jennifer S. Tsau, Jeffery D. Molkentin, Masaaki Komatsu, and Stephen M. Hedrick
In caspase 8-deficient mouse T cells, necroptosis occurs via a Ripk3- and Ripk1-dependent pathway independent of autophagy and programmed necrosis.
http://jem.rupress.org/cgi/content/abstract/208/4/633?etoc

Poly(ADP-Ribose) (PAR) Binding to Apoptosis-Inducing Factor Is Critical for PAR Polymerase-1-Dependent Cell Death (Parthanatos)
Yingfei Wang, No Soo Kim, Jean-Francois Haince, Ho Chul Kang, Karen K. David, Shaida A. Andrabi, Guy G. Poirier, Valina L. Dawson, and Ted M. Dawson
http://stke.sciencemag.org/cgi/content/abstract/sigtrans;4/167/ra20?etoc

Activation of p53 by Nutlin-3a Induces Apoptosis and Cellular Senescence in Human Glioblastoma Multiforme
Ruth Villalonga-Planells, Llorenç Coll-Mulet, Fina Martínez-Soler, Esther Castaño, Juan-Jose Acebes, Pepita Giménez-Bonafé, Joan Gil, Avelina Tortosa
http://www.plosone.org/article/info:doi/10.1371/journal.pone.0018588

Dimerization of Smac is crucial for its mitochondrial retention by XIAP subsequent to mitochondrial outer membrane permeabilization
Lorna Flanagan, Jordi Sebastia, Maria Eugenia Delgado, Jennifer C. Lennon, Markus Rehm
http://dx.doi.org/10.1016/j.bbamcr.2011.02.011

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Reviews
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The Open Cell Signaling Journal special issue:
“Life and death: A cell signaling prospective”

– Editorial
John Silke
http://www.benthamscience.com/open/tocellsj/articles/V003/SI0001TOCELLSJ/1TOCELLSJ.pdf

– Interplay of Bcl-2 Proteins Decides the Life or Death Fate
Grant Dewson
http://www.benthamscience.com/open/tocellsj/articles/V003/SI0001TOCELLSJ/3TOCELLSJ.htm

– A Prickly Subject: Apoptotic Regulation by Hedgehog Morphogens
Mark Ditzel
http://www.benthamscience.com/open/tocellsj/articles/V003/SI0001TOCELLSJ/9TOCELLSJ.htm

– Cytokine Deprivation and Cell Death
Paul G. Ekert and Anissa M. Jabbour
http://www.benthamscience.com/open/tocellsj/articles/V003/SI0001TOCELLSJ/20TOCELLSJ.htm

– Dual Philosophy in Death Receptor Signalling
Chahrazade Kantari and Henning Walczak
http://www.benthamscience.com/open/tocellsj/articles/V003/SI0001TOCELLSJ/27TOCELLSJ.htm

– Scorched Earth or Viral Birth?
Ian Gentle and Ueli Nachbur
http://www.benthamscience.com/open/tocellsj/articles/V003/SI0001TOCELLSJ/35TOCELLSJ.htm

– Dying for Something to Eat: How Cells Respond to Starvation
Alfredo Caro-Maldonado and Cristina Muñoz-Pinedo
http://www.benthamscience.com/open/tocellsj/articles/V003/SI0001TOCELLSJ/42TOCELLSJ.htm

Armed response: how dying cells influence T-cell functions
Ferguson, Thomas A.; Choi, Jayoung; Green, Douglas R.
http://onlinelibrary.wiley.com/doi/10.1111/j.1600-065X.2011.01006.x/abstract

Signaling cell death from the endoplasmic reticulum stress response
Gordon C Shore, Feroz R Papa, Scott A Oakes
http://dx.doi.org/10.1016/j.ceb.2010.11.003

Regulation of mitochondrial metabolism: yet another facet in the biology of the oncoprotein Bcl 2
Shefali Krishna, Ivan Cherh Chiet Low and Shazib Pervaiz
http://www.biochemj.org/bj/435/bj4350545.htm

Apoptosis promotes early tumorigenesis
D Tang, M T Lotze, R Kang and H J Zeh
http://www.nature.com/onc/journal/v30/n16/full/onc2010573a.html

Programmed Necrosis, Not Apoptosis, in the Heart
Kung, Gloria; Konstantinidis, Klitos; Kitsis, Richard N.
http://circres.ahajournals.org/cgi/pmidlookup?view=long&pmid=21493924

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News and views / other
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Retraction
Retraction Notice to: DNA-PKcs-PIDDosome: A Nuclear Caspase-2-Activating Complex with Role in G2/M Checkpoint Maintenance
M. Shi, C.J. Vivian, K.-J. Lee, C. Ge, K. Morotomi-Yano, C. Manzl, F. Bock, S. Sato, C. Tomomori-Sato, R. Zhu, J.S. Haug, S.K. Swanson, M.P. Washburn, D.J. Chen, B.P.C. Chen, A. Villunger, L. Florens, and C. Du
http://www.cell.com/fulltext/S0092-8674%2811%2900292-3

Autophagy in Ras-Induced Malignant Transformation: Fatal or Vital?
G. Mariño, I. Martins, and G. Kroemer
http://dx.doi.org/10.1016/j.molcel.2011.03.003

Traveling Bax and Forth from Mitochondria to Control Apoptosis
M.E. Soriano and L. Scorrano
http://www.cell.com/abstract/S0092-8674%2811%2900302-3

MCL1 meets its end during mitotic arrest
Scott E Millman and Michele Pagano
http://www.nature.com/embor/journal/v12/n5/full/embor201162a.html

Compartmentalized regulation of autophagy regulators: fine-tuning AMBRA1 by Bcl-2
Sharon ATooze and Patrice Codogno
http://www.nature.com/emboj/journal/v30/n7/abs/emboj201175a.html

Activated by Caspases
Wei Wong
Caspase activity in microglia does not trigger cell death, but rather induces proinflammatory responses.
http://stke.sciencemag.org/cgi/content/abstract/sigtrans;4/170/ec115?etoc

Jurg Tschopp 1951-2011
Ralph C Budd, Pascal Schneider, Fabienne Mackay and Andreas Strasser
http://www.nature.com/ni/journal/v12/n5/full/ni0511-367.html?WT.ec_id=NI-201105

Jürg Tschopp (1951–2011) ▶
Immunologist whose discoveries transformed patients’ lives.
http://www.nature.com/nature/journal/v472/n7343/full/472296a.html

Jürg Tschopp (1951-2011)
J. Browning and C. Ware
http://www.cell.com/immunity/fulltext/S1074-7613%2811%2900135-X

Apolist – january 2011

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BCL-2 FAMILY PROTEINS
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Reconstitution of proapoptotic BAK function in liposomes reveals a dual role for mitochondrial lipids in the BAK-driven membrane permeabilization process
Olatz Landeta, Ane Landajuela, David Gil, Stefka Taneva, Carmelo DiPrimo, Begoña Sot, Mikel Valle, Vadim Frolov, and Gorka Basañez
http://www.jbc.org/cgi/content/abstract/M110.165852v1

The Soluble Form of Bax Regulates Mitochondrial Fusion via MFN2 Homotypic Complexes
S. Hoppins, F. Edlich, M.M. Cleland, S. Banerjee, J.M. McCaffery, R.J. Youle, and J. Nunnari
http://www.cell.com/molecular-cell/abstract/S1097-2765%2810%2900916-0

Mutations to Bax beyond the BH3 domain disrupts interactions with pro-survival proteins and promotes apoptosis
Peter E. Czabotar, Erinna F. Lee, Geoff V. Thompson, Ahmad Z. Wardak, W. Douglas Fairlie, and Peter M. Colman
http://www.jbc.org/cgi/content/abstract/M110.161281v1

The BH3 Mimetic ABT-737 Induces Cancer Cell Senescence
Jin H. Song, Karthikeyan Kandasamy, Marina Zemskova, Ying-Wei Lin, and Andrew S. Kraft
http://cancerres.aacrjournals.org/cgi/content/abstract/71/2/506

Obatoclax induces Atg7-dependent autophagy independent of beclin-1 and BAX/BAK
F McCoy, J Hurwitz, N McTavish, I Paul, C Barnes, B O’Hagan, K Odrzywol, J Murray, D Longley, G McKerr and D A Fennell
http://www.nature.com/cddis/journal/v1/n12/full/cddis201086a.html

Susceptibility of Hep3B cells in different phases of cell cycle to tBid
Shi-Hong Ma, George G. Chen, Caiguo Ye, Billy C.S. Leung, Rocky L.K. Ho, Paul B.S. Lai
http://dx.doi.org/10.1016/j.bbamcr.2010.10.009

Cyclic-AMP-dependent protein kinase A regulates apoptosis by stabilizing the BH3-only protein Bim
Diane Moujalled, Ross Weston, Holly Anderton, Robert Ninnis, Pranay Goel, Andrew Coley, David CS Huang, Li Wu, Andreas Strasser and Hamsa Puthalakath
http://www.nature.com/embor/journal/v12/n1/full/embor2010190a.html

Bcl-2 family interaction with the mitochondrial morphogenesis machinery
M M Cleland, K L Norris, M Karbowski, C Wang, D-F Suen, S Jiao, N M George, X Luo, Z Li and R J Youle
http://www.nature.com/cdd/journal/v18/n2/full/cdd201089a.html

Effective Caspase Inhibition Blocks Neutrophil Apoptosis and Reveals Mcl-1 as Both a Regulator and a Target of Neutrophil Caspase Activation
David J. Wardle, Joseph Burgon, Ian Sabroe, Colin D. Bingle, Moira K. B. Whyte, Stephen A. Renshaw
http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0015768

Characterization of a Novel Interaction between Bcl-2 Members Diva and Harakiri
Lorenzo Sborgi, Susana Barrera-Vilarmau, Patricia Obregón, Eva de Alba
http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0015575

miR-29b is activated during neuronal maturation and targets BH3-only genes to restrict apoptosis
Adam J. Kole, Vijay Swahari, Scott M. Hammond, and Mohanish Deshmukh
http://genesdev.cshlp.org/cgi/content/abstract/25/2/125

Evidence for a second messenger function of dUTP during Bax mediated apoptosis of yeast and mammalian cells   Original Research Article
Drew Williams, Grant Norman, Chamel Khoury, Naomi Metcalfe, Jennie Briard, Aimee Laporte, Sara Sheibani, Liam Portt, Craig A. Mandato, Michael T. Greenwood
http://dx.doi.org/10.1016/j.bbamcr.2010.11.021

MCL-1 is a stress sensor that regulates autophagy in a developmentally regulated manner
Marc Germain, Angela P Nguyen, J Nicole Le Grand, Nicole Arbour, Jacqueline L Vanderluit, David S Park, Joseph T Opferman and Ruth S Slack
http://www.nature.com/emboj/journal/v30/n2/full/emboj2010326a.html

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CASPASES
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Caspase-3 triggers early synaptic dysfunction in a mouse model of Alzheimer’s disease.
D’Amelio M, Cavallucci V, Middei S, Marchetti C, Pacioni S, Ferri A, Diamantini A, De Zio D, Carrara P, Battistini L, Moreno S, Bacci A, Ammassari-Teule M, Marie H, Cecconi F.
http://www.nature.com/neuro/journal/v14/n1/full/nn.2709.html

Giant unilamellar vesicles (GUVs) as a new tool for analysis of caspase-8/Bid-FL complex binding to cardiolipin and its functional activity
O Jalmar, A J García-Sáez, L Berland, F Gonzalvez and P X Petit
http://www.nature.com/cddis/journal/v1/n12/full/cddis201081a.html

Involvement of caspase-9 in autophagy-mediated cell survival pathway
Hyo-Soon, Jeong | Hye Yeon, Choi | Eung-Ryoung, Lee | Jung-Hyun, Kim | Kilsoo, Jeon | Hyun-Joo, Lee | Ssang-Goo, Cho
http://dx.doi.org/10.1016/j.bbamcr.2010.09.016

Loss of caspase-2 dependent apoptosis induces autophagy following mitochondria oxidative stress in primary cultures of young-adult cortical neurons
Meenakshi Tiwari, Marisa Lopez-Cruzan, William W. Morgan, and Brian Herman
http://www.jbc.org/cgi/content/abstract/M110.163824v1

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DEATH RECEPTORS
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Cellular FLIP(L) plays a survival role and regulates morphogenesis in breast epithelial cells.
Yerbes R, Palacios C, Reginato MJ, López-Rivas A.
http://dx.doi.org/10.1016/j.bbamcr.2010.10.003

Immune modulation by Fas ligand reverse signaling: lymphocyte proliferation is attenuated by the intracellular Fas ligand domain
Katharina Lückerath, Vladimir Kirkin, Inga Maria Melzer, Frederic B. Thalheimer, Dagmar Siele, Wiebke Milani, Thure Adler, Antonio Aguilar-Pimentel, Marion Horsch, Geert Michel, Johannes Beckers, Dirk H. Busch, Markus Ollert, Valerie Gailus-Durner, Helmut Fuchs, Martin Hrabe de Angelis, Frank J. T. Staal, Krishnaraj Rajalingam, Anne-Odile Hueber, Lothar J. Strobl, Ursula Zimber-Strobl, and Martin Zörnig
http://bloodjournal.hematologylibrary.org/cgi/content/abstract/117/2/519

Caspase-8 and caspase-7 sequentially mediate proteolytic activation of acid sphingomyelinase in TNF-R1 receptosomes
Bärbel Edelmann, Uwe Bertsch, Vladimir Tchikov, Supandi Winoto-Morbach, Cristiana Perrotta, Marten Jakob, Sabine Adam-Klages, Dieter Kabelitz and Stefan Schütze
http://www.nature.com/emboj/journal/v30/n2/full/emboj2010327a.html

FLIPL induces caspase 8 activity in the absence of interdomain caspase 8 cleavage and alters substrate specificity
Cristina Pop, Andrew Oberst, Marcin Drag, Bram J. Van Raam, Stefan J. Riedl, Douglas R. Green and Guy S. Salvesen
http://www.biochemj.org/bj/433/bj4330447.htm

Phosphorylation by polo-like kinase 1 induces the tumor-suppressing activity of FADD
M-S Jang, S-J Lee, C-J Kim, C-W Lee and E Kim
http://www.nature.com/onc/journal/v30/n4/abs/onc2010423a.html

———————————————–
MISCELLANEOUS
———————————————–

ARTS and Siah Collaborate in a Pathway for XIAP Degradation
J.B. Garrison, R.G. Correa, M. Gerlic, K.W. Yip, A. Krieg, C.M. Tamble, R. Shi, K. Welsh, S. Duggineni, Z. Huang, K. Ren, C. Du, and J.C. Reed
http://www.cell.com/molecular-cell/abstract/S1097-2765%2810%2900958-5

Necrostatin-1 ameliorates symptoms in R6/2 transgenic mouse model of Huntington’s disease
S Zhu, Y Zhang, G Bai and H Li
http://www.nature.com/cddis/journal/v2/n1/full/cddis201094a.html

Calcium-dependent activation and autolysis of Arabidopsis metacaspase 2d
Naohide Watanabe and Eric Lam
http://www.jbc.org/cgi/content/abstract/M110.194340v2

——————————–
REVIEWS / COMMENTS
——————————–

Anti-apoptosis and cell survival: A review
Liam Portt, Grant Norman, Caitlin Clapp, Matthew Greenwood, Michael T. Greenwood
http://dx.doi.org/10.1016/j.bbamcr.2010.10.010

Memory-Stealing Caspase
Wei Wong
Caspase-3 plays an apoptosis-independent role in the early pathogenesis of Alzheimer’s disease.
http://stke.sciencemag.org/cgi/content/abstract/sigtrans;4/154/ec2?etoc

Pyroptosis: Macrophage Suicide Exposes Hidden Invaders
I.E. Brodsky and R. Medzhitov
http://www.cell.com/current-biology/abstract/S0960-9822%2810%2901594-0

Snapshot
Extrinsic Apoptosis Pathways
I. Verbrugge, R.W. Johnstone, and M.J. Smyth
http://download.cell.com/pdf/PIIS0092867410014224.pdf?id=e16241398b8eb460:1a9608ff:12d95a3ba8f:773c1295380026111

Apolist – July 2010

——————————
Bcl-2 family members
——————————

Phosphorylation of Mcl-1 by CDK1–cyclin B1 initiates its Cdc20-dependent destruction during mitotic arrest
Margaret E Harley, Lindsey A Allan, Helen S Sanderson and Paul R Clarke
http://www.nature.com/emboj/journal/v29/n14/abs/emboj2010112a.html

Conformational changes in BAK, a pore-forming proapoptotic Bcl-2 family member, upon membrane insertion and direct evidence for the existence of BH3:BH3 contact interface in BAK homooligomers
Kyoung Joon Oh, Pawan Singh, Kyungro Lee, Kelly Foss, Shinyoub Lee, Minji Park, Steffi Lee, Sreevidya Aluvila, Matthew Park, Puja Singh, Ryung-Suk Kim, Jindrich Smyersky, and D. Eric Walters
http://www.jbc.org/cgi/content/abstract/M110.135293v1

TRAIL-activated stress kinases suppress apoptosis through transcriptional upregulation of MCL-1
J K Son, S Varadarajan and S B Bratton
http://www.nature.com/cdd/journal/v17/n8/full/cdd20109a.html

Bcl-XL represents a druggable molecular vulnerability during aurora B inhibitor-mediated polyploidization
O. Jameel Shah, Xiaoyu Lin, Leiming Li, Xiaoli Huang, Junling Li, Mark G. Anderson, Hua Tang, Luis E. Rodriguez, Scott E. Warder, Shaun McLoughlin, Jun Chen, Joann Palma, Keith B. Glaser, Cherrie K. Donawho, Stephen W. Fesik, and Yu Shen
http://www.pnas.org/content/107/28/12634.abstract?etoc

Heightened mitochondrial priming is the basis for apoptotic hypersensitivity of CD4+ CD8+ thymocytes
Jeremy A. Ryan, Joslyn K. Brunelle, and Anthony Letai
http://www.pnas.org/content/107/29/12895.abstract?etoc

—————————————-
Death receptors and caspases
—————————————-

Fas-associated death domain (FADD) is a negative regulator of T-cell receptor–mediated necroptosis
Stephanie L. Osborn, Gretchen Diehl, Seong-Ji Han, Ling Xue, Nadia Kurd, Kristina Hsieh, Dragana Cado, Ellen A. Robey, and Astar Winoto
http://www.pnas.org/content/107/29/13034.abstract?etoc

Oncogenic Ras Diverts a Host TNF Tumor Suppressor Activity into Tumor Promoter
J.B. Cordero, J.P. Macagno, R.K. Stefanatos, K.E. Strathdee, R.L. Cagan, and M. Vidal
http://www.cell.com/developmental-cell/abstract/S1534-5807%2810%2900250-9

Gradients of a Ubiquitin E3 Ligase Inhibitor and a Caspase Inhibitor Determine Differentiation or Death in Spermatids
Y. Kaplan, L. Gibbs-Bar, Y. Kalifa, Y. Feinstein-Rotkopf, and E. Arama
http://www.cell.com/developmental-cell/abstract/S1534-5807%2810%2900299-6

——————–
Miscellaneous
——————–

From the Cover: Biophotonic probing of macromolecular transformations during apoptosis
Artem Pliss, Andrey N. Kuzmin, Aliaksandr V. Kachynski, and Paras N. Prasad
http://www.pnas.org/content/107/29/12771.abstract?etoc

HSP72 Protects Cells from ER Stress-induced Apoptosis via Enhancement of IRE1α-XBP1 Signaling through a Physical Interaction
Sanjeev Gupta, Ayswaria Deepti, Shane Deegan, Fernanda Lisbona, Claudio Hetz, Afshin Samali
http://www.plosbiology.org/article/info%3Adoi%2F10.1371%2Fjournal.pbio.1000410

————–
Reviews
————–

IAPs: from caspase inhibitors to modulators of NF-κB, inflammation and cancer
Mads Gyrd-Hansen & Pascal Meier
http://www.nature.com/nrc/journal/v10/n8/full/nrc2889.html

Intertwined pathways of programmed cell death in immunity
Stephen M. Hedrick 1 , Irene L. Ch’en 1 , Bryce N. Alves
http://www3.interscience.wiley.com/cgi-bin/fulltext/123526684/HTMLSTART

Cholesterol and peroxidized cardiolipin in mitochondrial membrane properties, permeabilization and cell death.
Montero J, Mari M, Colell A, Morales A, Basañez G, Garcia-Ruiz C, Fernández-Checa JC.
http://dx.doi.org/10.1016/j.bbabio.2010.02.010

—————
Comments
—————

Metacaspases are not caspases – always doubt
M Enoksson and G S Salvesen
http://www.nature.com/cdd/journal/v17/n8/full/cdd201045a.html

Paradise revealed: first-class science rocked by the sound of the waves
G P Amarante-Mendes, K R Bortoluci, P T Bozza, R Chammas and J P B Viola
http://www.nature.com/cdd/journal/v17/n8/abs/cdd201066a.html

Stalling in mitosis and releasing the apoptotic brake
Manabu Kurokawa and Sally Kornbluth
http://www.nature.com/emboj/journal/v29/n14/full/emboj2010150a.html

———————–

Bcl-2 family members

———————–

Phosphorylation of Mcl-1 by CDK1–cyclin B1 initiates its Cdc20-dependent destruction during mitotic arrest

Margaret E Harley, Lindsey A Allan, Helen S Sanderson and Paul R Clarke

http://www.nature.com/emboj/journal/v29/n14/abs/emboj2010112a.html

Conformational changes in BAK, a pore-forming proapoptotic Bcl-2 family member, upon membrane insertion and direct evidence for the existence of BH3:BH3 contact interface in BAK homooligomers

Kyoung Joon Oh, Pawan Singh, Kyungro Lee, Kelly Foss, Shinyoub Lee, Minji Park, Steffi Lee, Sreevidya Aluvila, Matthew Park, Puja Singh, Ryung-Suk Kim, Jindrich Smyersky, and D. Eric Walters

http://www.jbc.org/cgi/content/abstract/M110.135293v1

TRAIL-activated stress kinases suppress apoptosis through transcriptional upregulation of MCL-1

J K Son, S Varadarajan and S B Bratton

http://www.nature.com/cdd/journal/v17/n8/full/cdd20109a.html

Bcl-XL represents a druggable molecular vulnerability during aurora B inhibitor-mediated polyploidization

O. Jameel Shah, Xiaoyu Lin, Leiming Li, Xiaoli Huang, Junling Li, Mark G. Anderson, Hua Tang, Luis E. Rodriguez, Scott E. Warder, Shaun McLoughlin, Jun Chen, Joann Palma, Keith B. Glaser, Cherrie K. Donawho, Stephen W. Fesik, and Yu Shen

http://www.pnas.org/content/107/28/12634.abstract?etoc

Heightened mitochondrial priming is the basis for apoptotic hypersensitivity of CD4+ CD8+ thymocytes

Jeremy A. Ryan, Joslyn K. Brunelle, and Anthony Letai

http://www.pnas.org/content/107/29/12895.abstract?etoc

——————————

Death receptors and caspases

——————————

Fas-associated death domain (FADD) is a negative regulator of T-cell receptor–mediated necroptosis

Stephanie L. Osborn, Gretchen Diehl, Seong-Ji Han, Ling Xue, Nadia Kurd, Kristina Hsieh, Dragana Cado, Ellen A. Robey, and Astar Winoto

http://www.pnas.org/content/107/29/13034.abstract?etoc

Oncogenic Ras Diverts a Host TNF Tumor Suppressor Activity into Tumor Promoter

J.B. Cordero, J.P. Macagno, R.K. Stefanatos, K.E. Strathdee, R.L. Cagan, and M. Vidal

http://www.cell.com/developmental-cell/abstract/S1534-5807%2810%2900250-9

Gradients of a Ubiquitin E3 Ligase Inhibitor and a Caspase Inhibitor Determine Differentiation or Death in Spermatids

Y. Kaplan, L. Gibbs-Bar, Y. Kalifa, Y. Feinstein-Rotkopf, and E. Arama

http://www.cell.com/developmental-cell/abstract/S1534-5807%2810%2900299-6

————–

Miscellaneous

————–

From the Cover: Biophotonic probing of macromolecular transformations during apoptosis

Artem Pliss, Andrey N. Kuzmin, Aliaksandr V. Kachynski, and Paras N. Prasad

http://www.pnas.org/content/107/29/12771.abstract?etoc

HSP72 Protects Cells from ER Stress-induced Apoptosis via Enhancement of IRE1α-XBP1 Signaling through a Physical Interaction

Sanjeev Gupta, Ayswaria Deepti, Shane Deegan, Fernanda Lisbona, Claudio Hetz, Afshin Samali

http://www.plosbiology.org/article/info%3Adoi%2F10.1371%2Fjournal.pbio.1000410

———

Reviews

———

IAPs: from caspase inhibitors to modulators of NF-κB, inflammation and cancer

Mads Gyrd-Hansen & Pascal Meier

http://www.nature.com/nrc/journal/v10/n8/full/nrc2889.html

Intertwined pathways of programmed cell death in immunity

Stephen M. Hedrick 1 , Irene L. Ch’en 1 , Bryce N. Alves

http://www3.interscience.wiley.com/cgi-bin/fulltext/123526684/HTMLSTART

Cholesterol and peroxidized cardiolipin in mitochondrial membrane properties, permeabilization and cell death.

Montero J, Mari M, Colell A, Morales A, Basañez G, Garcia-Ruiz C, Fernández-Checa JC.

http://dx.doi.org/10.1016/j.bbabio.2010.02.010

———–

Comments

———–

Metacaspases are not caspases – always doubt

M Enoksson and G S Salvesen

http://www.nature.com/cdd/journal/v17/n8/full/cdd201045a.html

Paradise revealed: first-class science rocked by the sound of the waves

G P Amarante-Mendes, K R Bortoluci, P T Bozza, R Chammas and J P B Viola

http://www.nature.com/cdd/journal/v17/n8/abs/cdd201066a.html

Stalling in mitosis and releasing the apoptotic brake

Manabu Kurokawa and Sally Kornbluth

http://www.nature.com/emboj/journal/v29/n14/full/emboj2010150a.html

Apolist – june 2010

————————
Bcl-2 family proteins
————————-

Apoptosis Threshold Set by Noxa and Mcl-1 after T Cell Activation Regulates Competitive Selection of High-Affinity Clones
F.M. Wensveen, K.P.J.M. van Gisbergen, I.A.M. Derks, C. Gerlach, T.N. Schumacher, R.A.W. van Lier, and E. Eldering
http://www.cell.com/immunity/abstract/S1074-7613%2810%2900208-6

Growth factor stimulation induces cell survival by C-jun/ATF2-dependent activation of BCL-XL
Ahmad Salameh, Federico Galvagni, Francesca Anselmi, Caterina De Clemente, Maurizio Orlandini, and Salvatore Oliviero
J. Biol. Chem. published 27 May 2010, 10.1074/jbc.M109.087221
http://www.jbc.org/cgi/content/abstract/M109.087221v1

A genome-wide RNA interference screen reveals an essential CREB3L2-ATF5-MCL1 survival pathway in malignant glioma with therapeutic implications
Zhi Sheng, Li Li, Lihua J Zhu, Thomas W Smith, Andrea Demers, Alonzo H Ross, Richard P Moser and Michael R Green
http://www.nature.com/nm/journal/v16/n6/full/nm.2158.html

The proapoptotic BH3-only protein Bim is downregulated in a subset of colorectal cancers and is repressed by antiapoptotic COX-2/PGE2 signalling in colorectal adenoma cells
A Greenhough, C A Wallam, D J Hicks, M Moorghen, A C Williams and C Paraskeva
http://www.nature.com/onc/journal/v29/n23/full/onc201094a.html

Deletion of proapoptotic Puma selectively protects hematopoietic stem and progenitor cells against high-dose radiation
Lijian Shao, Yan Sun, Zhonghui Zhang, Wei Feng, Yongxing Gao, Zailong Cai, Zack Z. Wang, A. Thomas Look, and Wen-Shu Wu
Blood 2010;115 4707-4714
http://bloodjournal.hematologylibrary.org/cgi/content/abstract/115/23/4707

BH3 mimetics antagonizing restricted prosurvival Bcl-2 proteins represent another class of selective immune modulatory drugs
Emma M. Carrington, Ingela B. Vikstrom, Amanda Light, Robyn M. Sutherland, Sarah L. Londrigan, Kylie D. Mason, David C. S. Huang, Andrew M. Lew, and David M. Tarlinton
http://www.pnas.org/content/107/24/10967.abstract?etoc

The BH3-mimetic gossypol induces both beclin 1-dependent and beclin 1-independent cytoprotective autophagy in cancer cells
Ping Gao, Chantal Bauvy, Sylvie Souquere, Giovanni Tonelli, Lei Liu, Yushan Zhu, Zhenzhen Qiao, Daniela Bakula, Tassula Proikas-Cezanne, Gerard Pierron, Patrice Codogno, Quan Chen, and Maryam Mehrpour
J. Biol. Chem. published 7 June 2010, 10.1074/jbc.M110.118125
http://www.jbc.org/cgi/content/abstract/M110.118125v1

BCL-2 and bax interact via the BH1-3 groove:BH3 motif interface and a novel interface involving the BH4 motif
Jingzhen Ding, Zhi Zhang, G. Jane Roberts, Mina Falcone, Yiwei Miao, Yuanlong Shao, Xuejun C. Zhang, David W. Andrews, and Jialing Lin
J. Biol. Chem. published 28 June 2010, 10.1074/jbc.M110.148361
http://www.jbc.org/cgi/content/abstract/M110.148361v1

High-Mobility Group A1 Proteins Regulate p53-Mediated Transcription of Bcl-2 Gene
Francesco Esposito, Mara Tornincasa, Paolo Chieffi, Ivana De Martino, Giovanna Maria Pierantoni, and Alfredo Fusco
Cancer Res 2010;70 5379-5388
http://cancerres.aacrjournals.org/cgi/content/abstract/70/13/5379

————————-
Death receptors and IAPs
————————-

XIAP impairs Smac release from the mitochondria during apoptosis
L Flanagan, J Sebastià, L P Tuffy, A Spring, A Lichawska, M Devocelle, J H M Prehn and M Rehm
http://www.nature.com/cddis/journal/v1/n6/full/cddis201026a.html

FADD-calmodulin interaction: A novel player in cell cycle regulation
Pages 898-911
Giuliana Papoff, Nadia Trivieri, Roberta Crielesi, Francesca Ruberti, Sonia Marsilio, Giovina Ruberti
http://dx.doi.org/10.1016/j.bbamcr.2010.04.006

Effective Blockage of Both the Extrinsic and Intrinsic Pathways of Apoptosis in Mice by TAT-crmA
Stefan Krautwald, Ekkehard Ziegler, Lars Rölver, Andreas Linkermann, Kirsten A. Keyser, Philip Steen, Kai C. Wollert, Mortimer Korf-Klingebiel, and Ulrich Kunzendorf
http://www.jbc.org/content/285/26/19997.abstract?etoc

Sphingosine-1-phosphate is a missing cofactor for the E3 ubiquitin ligase TRAF2
Sergio E. Alvarez, Kuzhuvelil B. Harikumar,Nitai C. Hait,Jeremy Allegood,Graham M. Strub,Eugene Y. Kim,Michael Maceyka,Hualiang Jiang, Cheng Luo, Tomasz Kordula, Sheldon Milstien & Sarah Spiegel
http://www.nature.com/nature/journal/v465/n7301/full/nature09128.html

mir-200c Regulates Induction of Apoptosis through CD95 by Targeting FAP-1
R. Schickel, S.-M. Park, A.E. Murmann, and M.E. Peter
http://www.cell.com/molecular-cell/abstract/S1097-2765%2810%2900380-1

Overcoming cancer cell resistance to Smac mimetic induced apoptosis by modulating cIAP-2 expression
Sean L. Petersen, Michael Peyton, John D. Minna, and Xiaodong Wang
http://www.pnas.org/content/107/26/11936.abstract?etoc

————————-
Miscellaneous
————————-

Activation of autophagy during cell death requires the engulfment receptor Draper
Christina K. McPhee, Mary A. Logan, Marc R. Freeman and Eric H. Baehrecke
http://www.nature.com/nature/journal/v465/n7301/full/nature09127.html

Lysosomal membrane permeabilization and cathepsin release is a Bax/Bak-dependent, amplifying event of apoptosis in fibroblasts and monocytes
C Oberle, J Huai, T Reinheckel, M Tacke, M Rassner, P G Ekert, J Buellesbach and C Borner
http://www.nature.com/cdd/journal/v17/n7/full/cdd2009214a.html

Oncogene-Induced Sensitization to Chemotherapy-Induced Death Requires Induction as well as Deregulation of E2F1
G. Vignir Helgason, Jim O’Prey, and Kevin M. Ryan
Cancer Res 2010;70 4074-4080
http://cancerres.aacrjournals.org/cgi/content/abstract/70/10/4074

Identification of functional regions defining different activity between caspase-3 and caspase-7 within cells
Hirokazu Nakatsumi and Shin Yonehara
J. Biol. Chem. published 21 June 2010, 10.1074/jbc.M110.126573
http://www.jbc.org/cgi/content/abstract/M110.126573v1

————————-
REVIEWS / COMMENTS
————————-

Bcl-2-regulated cell death signalling in the prevention of autoimmunity
D Tischner, C Woess, E Ottina and A Villunger
http://www.nature.com/cddis/journal/v1/n6/full/cddis201027a.html

The role of caspase-2 in stress-induced apoptosis
Lisa Bouchier-Hayes
http://www3.interscience.wiley.com/journal/123286432/abstract

Neuronal caspase-3 signaling: not only cell death
M D’Amelio, V Cavallucci and F Cecconi
http://www.nature.com/cdd/journal/v17/n7/full/cdd2009180a.html

Clearance of apoptotic cells: implications in health and disease
Michael R. Elliott and Kodi S. Ravichandran
http://jcb.rupress.org/cgi/content/abstract/189/7/1059?etoc

Only the Strong Survive
A. Villunger
http://www.cell.com/immunity/abstract/S1074-7613%2810%2900213-X

Depressed About Caspases?
Elizabeth M. Adler
Sci. Signal. 3 (125), ec170. [DOI: 10.1126/scisignal.3125ec170]
Elements of the mitochondrial apoptosis pathway are used to mediate long-term depression of synaptic function.
http://stke.sciencemag.org/cgi/content/abstract/sigtrans;3/125/ec170?etoc

Apolist – april 2010

DeathBase: a database on structure, evolution and function of proteins involved in apoptosis and other forms of cell death
J Díez, D Walter, C Muñoz-Pinedo and T Gabaldón
http://www.nature.com/cdd/journal/v17/n5/full/cdd2009215a.html
http://www.deathbase.org

BCL-2 PROTEINS

Mtd/Bok takes a swing: proapoptotic Mtd/Bok regulates trophoblast cell proliferation during human placental development and in preeclampsia
J E Ray, J Garcia, A Jurisicova and I Caniggia
http://www.nature.com/cdd/journal/v17/n5/full/cdd2009167a.html

AMP kinase-mediated activation of the BH3-only protein Bim couples energy depletion to stress-induced apoptosis
Caoimhín G. Concannon, Liam P. Tuffy, Petronela Weisová, Helena P. Bonner, David Dávila, Caroline Bonner, Marc C. Devocelle, Andreas Strasser, Manus W. Ward, and Jochen H.M. Prehn
http://jcb.rupress.org/cgi/content/abstract/189/1/83?etoc

Acquired resistance to ABT-737 in lymphoma cells that up-regulate MCL-1 and BFL-1
Derek Yecies, Nicole E. Carlson, Jing Deng, and Anthony Letai
Blood 2010;115 3304-3313
http://bloodjournal.hematologylibrary.org/cgi/content/abstract/115/16/3304

Ceramide and activated Bax act synergistically to permeabilize the mitochondrial outer membrane
Vidyaramanan Ganesan, Meenu N. Perera, David Colombini, Debra Datskovskiy, Kirti Chadha & Marco Colombini
http://www.springerlink.com/content/v6473l4mr0257826/

Bax forms an oligomer via separate, yet interdependent, surfaces
Zhi Zhang, Weijia Zhu, Suzanne M. Lapolla, Yiwei Miao, Yuanlong Shao, Mina Falcone, Doug Boreham, Nicole McFarlane, Jingzhen Ding, Arthur E. Johnson, Xuejun C. Zhang, David W. Andrews, and Jialing Lin
http://www.jbc.org/cgi/content/abstract/M110.113456v1

BH3 response profiles from neuroblastoma mitochondria predict activity of small molecule Bcl-2 family antagonists
K C Goldsmith, B J Lestini, M Gross, L Ip, A Bhumbla, X Zhang, H Zhao, X Liu and M D Hogarty
http://www.nature.com/cdd/journal/v17/n5/full/cdd2009171a.html

Deletion of Puma protects hematopoietic stem cells and confers long-term survival in response to high-dose  -irradiation
Hui Yu, Hongmei Shen, Youzhong Yuan, Richard XuFeng, Xiaoxia Hu, Sean P. Garrison, Lin Zhang, Jian Yu, Gerard P. Zambetti, and Tao Cheng
http://bloodjournal.hematologylibrary.org/cgi/content/abstract/115/17/3472

Regulation of mitochondrial apoptotic events by p53-mediated disruption of complexes between anti-apoptotic Bcl-2 members and Bim
Jie Han, Leslie A. Goldstein, Wen Hou, Brian R. Gastman, and Hannah Rabinowich
http://www.jbc.org/cgi/content/abstract/M109.081042v1

IBRDC2, an IBR-type E3 ubiquitin ligase, is a regulatory factor for Bax and apoptosis activation
Giovanni Benard, Albert Neutzner, Guihong Peng, Chunxin Wang, Ferenc Livak, Richard J Youle and Mariusz Karbowski
http://www.nature.com/emboj/journal/v29/n8/full/emboj201039a.html

Apoptotic regulation by MCL-1 through hetero-dimerization
Qian Liu, Tudor Moldoveanu, Tara Sprules, Edna Matta-Camacho, Nura Mansur-Azzam, and Kalle Gehring
http://www.jbc.org/cgi/content/abstract/M110.105452v1

Defective ubiquitin-mediated degradation of antiapoptotic Bfl-1 predisposes to lymphoma
Gaofeng Fan, Matthew J. Simmons, Sheng Ge, Jui Dutta-Simmons, Jérôme Kucharczak, Yacov Ron, David Weissmann, Chiann-Chyi Chen, Chandreyee Mukherjee, Eileen White, and Céline Gélinas
http://bloodjournal.hematologylibrary.org/cgi/content/abstract/115/17/3559

Death Receptors and IAPs

Mitotic arrest and JNK-induced proteasomal degradation of FLIP and Mcl-1 are key events in the sensitization of breast tumor cells to TRAIL by antimicrotubule agents
T Sánchez-Pérez, G Ortiz-Ferrón and A López-Rivas
http://www.nature.com/cdd/journal/v17/n5/full/cdd2009176a.html

c-Flip overexpression affects satellite cell proliferation and promotes skeletal muscle aging
C Giampietri, S Petrungaro, P Coluccia, F Antonangeli, K Giannakakis, T Faraggiana, A Filippini, G Cossu and E Ziparo
http://www.nature.com/cddis/journal/v1/n4/full/cddis201017a.html

Extreme lymphoproliferative disease and fatal autoimmune thrombocytopenia in FasL and TRAIL double-deficient mice
Lisa M. Sedger, Arna Katewa, Ann K. Pettersen, Sarah R. Osvath, Geoff C. Farrell, Graeme J. Stewart, Linda J. Bendall, and Stephen I. Alexander
Blood 2010;115 3258-3268
http://bloodjournal.hematologylibrary.org/cgi/content/abstract/115/16/3258

Caspase-dependent generation of reactive oxygen species in human astrocytoma cells contributes to resistance to TRAIL-mediated apoptosis
K Choi, S-W Ryu, S Song, H Choi, S W Kang and C Choi
http://www.nature.com/cdd/journal/v17/n5/full/cdd2009154a.html

Crystal Structures of the TRAF2: cIAP2 and the TRAF1: TRAF2: cIAP2 Complexes: Affinity, Specificity, and Regulation
C. Zheng, V. Kabaleeswaran, Y. Wang, G. Cheng, and H. Wu
http://www.cell.com/molecular-cell/abstract/S1097-2765%2810%2900244-3

Inhibition of NF- B signaling by quinacrine is cytotoxic to human colon carcinoma cell lines (cc) and is synergistic in combination with TRAIL or oxaliplatin
Tanvi S. Jani, Jennifer DeVecchio, Tapati Mazumdar, Akwasi Agyeman, and Janet A. Houghton
J. Biol. Chem. published 27 April 2010, 10.1074/jbc.M109.091645
http://www.jbc.org/cgi/content/abstract/M109.091645v1

Chemoprevention of colorectal cancer by targeting APC-deficient cells for apoptosis
Ling Zhang1,6, Xiaoyang Ren1,6, Eckhard Alt2, Xiaowen Bai2, Shaoyi Huang1, Zhengming Xu1, Patrick M. Lynch3, Mary P. Moyer5, Xian-Feng Wen1 & Xiangwei Wu1,4
http://www.nature.com/nature/journal/v464/n7291/full/nature08871.html

CASPASES AND DOWNSTREAM

Caspase-Dependent Conversion of Dicer Ribonuclease into a Death-Promoting Deoxyribonuclease
A. Nakagawa et al.
http://www.sciencemag.org/cgi/content/abstract/328/5976/327

Crystal Structure of the Caenorhabditis elegans Apoptosome Reveals an Octameric Assembly of CED-4
S. Qi, Y. Pang, Q. Hu, Q. Liu, H. Li, Y. Zhou, T. He, Q. Liang, Y. Liu, X. Yuan, G. Luo, H. Li, J. Wang, N. Yan, and Y. Shi
http://dx.doi.org/10.1016/j.cell.2010.03.017

Caspases in virus-infected cells contribute to recognition by CD8(+) T lymphocytes.
López D, García-Calvo M, Smith GL, Del Val M.
http://www.jimmunol.org/cgi/content/full/184/9/5193

Matrix metalloproteinase-3 is increased and participates in neuronal apoptotic signaling downstream of caspase-12 during ER stress
Eun-Mee Kim, Eun-Jung Shin, Ji Hyun Choi, Hyo Jin Son, Il-Seon Park, Tong H. Joh, and Onyou Hwang
J. Biol. Chem. published 5 April 2010, 10.1074/jbc.M109.093799
http://www.jbc.org/cgi/content/abstract/M109.093799v1

Identification of two evolutionarily conserved genes regulating processing of engulfed apoptotic cells
Jason M. Kinchen and Kodi S. Ravichandran
http://www.nature.com/nature/journal/v464/n7289/full/nature08853.html

Caspase activation precedes and leads to tangles
Alix de Calignon1,2, Leora M. Fox1, Rose Pitstick3, George A. Carlson3, Brian J. Bacskai1, Tara L. Spires-Jones1 & Bradley T. Hyman
http://www.nature.com/nature/journal/v464/n7292/abs/nature08890.html?lang=en

Caspase-3 cleaves specific 19S proteasome subunits in skeletal muscle stimulating proteasome activity
Xiaonan H. Wang, Liping Zhang, William E. Mitch, Joseph M. LeDoux, Junping Hu, and Jie Du
J. Biol. Chem. published 27 April 2010, 10.1074/jbc.M109.041707
http://www.jbc.org/cgi/content/abstract/M109.041707v1

Cleavage of sphingosine kinase 2 by caspase-1 provokes its release from apoptotic cells
Andreas Weigert, Sarah Cremer, Martina Victoria Schmidt, Andreas von Knethen, Carlo Angioni, Gerd Geisslinger, and Bernhard Brüne
http://bloodjournal.hematologylibrary.org/cgi/content/abstract/115/17/3531

Granzyme B-induced and caspase 3-dependent cleavage of gelsolin by mouse cytotoxic T cells modifies cytoskeleton dynamics
Praxedis Martin, Julian Pardo, Natalie Schill, Lars Joeckel, Matthias Berg, Christopher J. Froelich, Reinhard Wallich, and Markus M. Simon
http://www.jbc.org/cgi/content/abstract/M109.056028v1

MISCELLANEOUS

Apoptosis and non-inflammatory phagocytosis can be induced by mitochondrial damage without caspases
M F van Delft, D P Smith, M H Lahoud, D C S Huang and J M Adams
http://www.nature.com/cdd/journal/v17/n5/abs/cdd2009166a.html

Involvement of JNK in the regulation of autophagic cell death
S Shimizu, A Konishi, Y Nishida, T Mizuta, H Nishina, A Yamamoto and Y Tsujimoto
http://www.nature.com/onc/journal/v29/n14/full/onc2009487a.html

Simultaneous Induction of Non-Canonical Autophagy and Apoptosis in Cancer Cells by ROS-Dependent ERK and JNK Activation
Chew Hooi Wong, Kartini Bte Iskandar, Sanjiv Kumar Yadav, Jayshree L. Hirpara, Thomas Loh, Shazib Pervaiz
http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0009996

The Cdc42/Par6/aPKC Polarity Complex Regulates Apoptosis-Induced Compensatory Proliferation in Epithelia
S.J. Warner, H. Yashiro, and G.D. Longmore
http://www.cell.com/current-biology/abstract/S0960-9822%2810%2900345-3

REVIEWS / COMMENTS

Processing by Caspases
John F. Foley
http://stke.sciencemag.org/cgi/content/abstract/sigtrans;3/119/ec125?etoc

Dicer’s Cut and Switch
Q. Liu and Z. Paroo
An enzyme that cleaves RNA is converted to a DNA-cleaving enzyme during programmed cell death in Caenorhabditis elegans.
http://www.sciencemag.org/cgi/content/summary/328/5976/314

The Apoptosome at High Resolution
X. Teng and J.M. Hardwick
http://www.cell.com/abstract/S0092-8674%2810%2900432-0

Bcl-2 antagonists and cancer: from the clinic, back to the bench
M Degli Esposti
http://www.nature.com/cddis/journal/v1/n4/full/cddis201015a.html

CK2: uncoupling apoptotic events
J Cell Sci 2010;123 e903
http://jcs.biologists.org/cgi/content/full/123/9/e903

Dependence receptors: a new paradigm in cell signaling and cancer therapy
D Goldschneider and P Mehlen
http://www.nature.com/onc/journal/v29/n13/full/onc201013a.html

Regulation of apoptosis-associated lysosomal membrane permeabilization
Ann-Charlotte Johansson, Hanna Appelqvist, Cathrine Nilsson, Katarina Kågedal, Karin Roberg & Karin Öllinger
http://www.springerlink.com/content/h73601w625348755/

Necroptosis as an alternative form of programmed cell death
Dana E Christofferson, Junying Yuan
http://dx.doi.org/10.1016/j.ceb.2009.12.003

Apolist – january 10

BCL-2 FAMILY PROTEINS

Deubiquitinase USP9X stabilizes MCL1 and promotes tumour cell survival
Martin Schwickart et al.
http://www.nature.com/nature/journal/v463/n7277/full/nature08646.html

Regulation of stress-induced nuclear protein redistribution: a new function of Bax and Bak uncoupled from Bcl-xL
L Lindenboim, E Blacher, C Borner and R Stein
http://www.nature.com/cdd/journal/v17/n2/abs/cdd2009145a.html

The Antiapoptotic Protein BCL2L1/BCL-XL is Neutralized by Proapoptotic PMAIP1/Noxa in Neuroblastoma Thereby Determining Bortezomib-Sensitivity Independent of Prosurvival MCL1 Expression
Judith Hagenbuchner, Michael J. Ausserlechner, Verena Porto, Reinhard David, Bernhard Meister, Martin Bodner, Andreas Villunger, Kathrin Geiger, and Petra Obexer
J. Biol. Chem. published 5 January 2010, 10.1074/jbc.M109.038331
http://www.jbc.org/cgi/content/abstract/M109.038331v1

Rheb GTPase controls apoptosis by regulating the interaction of FKBP38 with Bcl-2 and Bcl-XL
Dongzhu Ma, Xiaochun Bai, Huafei Zou, Yumei Lai, and Yu Jiang
J. Biol. Chem. published 4 January 2010, 10.1074/jbc.M109.092353
http://www.jbc.org/cgi/content/abstract/M109.092353v1

The Bax carboxy-terminal hydrophobic helix does not determine organelle-specific targeting but is essential for maintaining Bax in an inactive state and for stable mitochondrial membrane insertion
Stephanie E. Brock, Chi Li & Binks W. Wattenberg
http://www.springerlink.com/content/bkmqg7w044600051/

Mcl-1128–350 fragment induces apoptosis through direct interaction with Bax
Emmanuelle Ménoret, Patricia Gomez-Bougie, Sylvanie Surget, Valérie Trichet, Lisa Oliver, Catherine Pellat-Deceunynck, Martine Amiot
http://dx.doi.org/10.1016/j.febslet.2009.11.094

Myeloid progenitor cells lacking p53 exhibit delayed up-regulation of Puma and prolonged survival after cytokine deprivation
Anissa M. Jabbour, Carmel P. Daunt, Benjamin D. Green, Sandra Vogel, Lavinia Gordon, Rachel S. Lee, Natasha Silke, Richard B. Pearson, Cassandra J. Vandenberg, Priscilla N. Kelly, Stephen L. Nutt, Andreas Strasser, Christoph Borner, and Paul G. Ekert
Blood 2010;115 344-352
http://bloodjournal.hematologylibrary.org/cgi/content/abstract/115/2/344

Interleukin-7 Regulates Bim Proapoptotic Activity in Peripheral T-Cell Survival
Wen Qing Li, Tad Guszczynski, Julie A. Hixon, and Scott K. Durum
Mol. Cell. Biol. 2010;30 590-600
http://mcb.asm.org/cgi/content/abstract/30/3/590

Cyclin-Dependent Kinase 1-Mediated Bcl-xL/Bcl-2 Phosphorylation Acts as a Functional Link Coupling Mitotic Arrest and Apoptosis
David T. Terrano, Meenakshi Upreti, and Timothy C. Chambers
Mol. Cell. Biol. 2010;30 640-656
http://mcb.asm.org/cgi/content/abstract/30/3/640

Differential Dependence on Beclin 1 for the Regulation of Pro-Survival Autophagy by Bcl-2 and Bcl-xL in HCT116 Colorectal Cancer Cells
Muriel Priault, Erika Hue, Fanny Marhuenda, Paul Pilet, Lisa Oliver, François M. Vallette
http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0008755

Prevention of premature senescence requires JNK regulation of Bcl-2 and reactive oxygen species
J -J Lee, J -H Lee, Y -G Ko, S I Hong and J -S Lee
http://www.nature.com/onc/journal/v29/n4/abs/onc2009355a.html

.

Death receptors and IAPs

Caspase-Mediated Cleavage, IAP Binding, and Ubiquitination: Linking Three Mechanisms Crucial for Drosophila NF-κB Signaling
N. Paquette, M. Broemer, K. Aggarwal, L. Chen, M. Husson, D. Ertürk-Hasdemir, J.-M. Reichhart, P. Meier, and N. Silverman
http://www.cell.com/molecular-cell/abstract/S1097-2765(10)00039-0

TAK1 Is Required for Survival of Mouse Fibroblasts Treated with TRAIL, and Does So by NF-κB Dependent Induction of cFLIPL
Josep Maria Lluis, Ulrich Nachbur, Wendy Diane Cook, Ian Edward Gentle, Donia Moujalled, Maryline Moulin, Wendy Wei-Lynn Wong, Nufail Khan, Diep Chau, Bernard Andrew Callus, James Edward Vince, John Silke, David Lawrence Vaux
http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0008620

Akt promotes chemoresistance in human ovarian cancer cells by modulating cisplatin-induced, p53-dependent ubiquitination of FLICE-like inhibitory protein
M R Abedini, E J Muller, R Bergeron, D A Gray and B K Tsang
http://www.nature.com/onc/journal/v29/n1/abs/onc2009300a.html

Histone deacetylase inhibitors induce thyroid cancer-specific apoptosis through proteasome-dependent inhibition of TRAIL degradation
E Borbone, M T Berlingieri, F De Bellis, A Nebbioso, G Chiappetta, A Mai, L Altucci and A Fusco
http://www.nature.com/onc/journal/v29/n1/abs/onc2009306a.html

Avicin D, a Plant Triterpenoid, Induces Cell Apoptosis by Recruitment of Fas and Downstream Signaling Molecules into Lipid Rafts
Zhi-Xiang Xu, Tian Ding, Valsala Haridas, Fiona Connolly, Jordan U. Gutterman
http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0008532

IAP Regulation of Metastasis
S. Mehrotra, L.R. Languino, C.M. Raskett, A.M. Mercurio, T. Dohi, and D.C. Altieri
http://www.cell.com/cancer-cell/abstract/S1535-6108%2809%2900422-X

Targeting a novel N-terminal epitope of death receptor 5 triggers tumor cell death
Peng Zhang, Yong Zheng, Juan Shi, Yaxi Zhang, Shilian Liu, Yanxin Liu, and Dexian Zheng
J. Biol. Chem. published 27 January 2010, 10.1074/jbc.M109.070680
http://www.jbc.org/cgi/content/abstract/M109.070680v1

Multivalent DR5 Peptides Activate the TRAIL Death Pathway and Exert Tumoricidal Activity
Valeria Pavet, Julien Beyrath, Christophe Pardin, Alexandre Morizot, Marie-Charlotte Lechner, Jean-Paul Briand, Miriam Wendland, Wolfgang Maison, Sylvie Fournel, Olivier Micheau, Gilles Guichard, and Hinrich Gronemeyer
Cancer Res 2010;70 1101-1110
http://cancerres.aacrjournals.org/cgi/content/abstract/70/3/1101

Tumor necrosis factor–related apoptosis-inducing ligand 1 (TRAIL1) enhances the transition of red blood cells from the larval to adult type during metamorphosis in Xenopus
Kei Tamura, Shuuji Mawaribuchi, Shin Yoshimoto, Tadayoshi Shiba, Nobuhiko Takamatsu, and Michihiko Ito
Blood 2010;115 850-859
http://bloodjournal.hematologylibrary.org/cgi/content/abstract/115/4/850

.

Apoptotic process

Inhibition of a protein kinase Akt1 by apoptosis signal-regulating kinase-1 (ASK1) is involved in apoptotic inhibition of regulatory volume increase
Muthangi Subramanyam, Nobuyuki Takahashi, Yuichi Hasegawa, Tatsuma Mohri, and Yasunobu Okada
J. Biol. Chem. published 4 January 2010, 10.1074/jbc.M109.072785
http://www.jbc.org/cgi/content/abstract/M109.072785v1

Apoptosis blocks Beclin 1-dependent autophagosome synthesis: an effect rescued by Bcl-xL
S Luo and D C Rubinsztein
http://www.nature.com/cdd/journal/v17/n2/abs/cdd2009121a.html

Engineering a polarity-sensitive biosensor for time-lapse imaging of apoptotic processes and degeneration pp67 – 73
Yujin E Kim, Jeannie Chen, Jonah R Chan and Ralf Langen
http://www.nature.com/nmeth/journal/v7/n1/abs/nmeth.1405.html?lang=en

.

OTHER

Dynein light chain 1 is required for autophagy, protein clearance, and cell death in Drosophila
Yakup Batlevi, Damali N. Martin, Udai Bhan Pandey, Claudio R. Simon, Christine M. Powers, J. Paul Taylor, and Eric H. Baehrecke
http://www.pnas.org/cgi/content/abstract/107/2/742?etoc

Rab5 Mediates Caspase-8–promoted Cell Motility and Metastasis
Vicente A. Torres, Ainhoa Mielgo, Simone Barbero, Ruth Hsiao, John A. Wilkins, and Dwayne G. Stupack
http://www.molbiolcell.org/cgi/content/abstract/21/2/369?etoc

The apoptotic machinery as a biological complex system: analysis of its omics and evolution, identification of candidate genes for fourteen major types of cancer, and experimental validation in CML and neuroblastoma
Di Pietro, C; Ragusa, M; Barbagallo, D; Duro, LR; Guglielmino, MR; Majorana, A; Angelica, R; Scalia, M; Statello, L; Salito, L; Tomasello, L; Pernagallo, S; Valenti, S; D’Agostino, V; Triberio, P; Tandurella, I; Palumbo, GA; La Cava, P; Cafiso, V; Bertuccio, T; Santagati, M; Destri, GL; Lanzafame, S; Di Raimondo, F; Stefani, S; Mishra, B; Purrello, M
http://www.biomedcentral.com/1755-8794/2/20

Positive selection on apoptosis related genes
Rute R. da Fonseca, Carolin Kosiol, Tomáš Vinař, Adam Siepel, Rasmus Nielsen
http://dx.doi.org/10.1016/j.febslet.2009.12.022

Coupling of the cell cycle and apoptotic machineries in developing T cells
Ling Xue, Yuefang Sun, Leslie Chiang, Bo He, Chulho Kang, Hector Nolla, and Astar Winoto
J. Biol. Chem. published 12 January 2010, 10.1074/jbc.M109.035535
http://www.jbc.org/cgi/content/abstract/M109.035535v1

p53 Controls Radiation-Induced Gastrointestinal Syndrome in Mice Independent of Apoptosis
D. G. Kirsch et al.
http://www.sciencemag.org/cgi/content/abstract/327/5965/593

.
Reviews

Several reviews on microRNAs and cell death/cancer in CDD:
MicroRNAs meet cell death
G Melino and R A Knight
http://www.nature.com/cdd/journal/v17/n2/full/cdd2009122a.html

Cellular and nuclear degradation during apoptosis
Pages 900-912
Bin He, Nan Lu, Zheng Zhou
http://dx.doi.org/10.1016/j.ceb.2009.08.008

Modulation of apoptosis by early human papillomavirus proteins in cervical cancer
A. Lagunas-Martínez, V. Madrid-Marina, P. Gariglio
http://dx.doi.org/10.1016/j.bbcan.2009.03.005

Transcription-independent p53 apoptosis: an alternative route to death
Daniel Speidel
http://www.cell.com/trends/cell-biology/abstract/S0962-8924(09)00240-2

Apolist – december 09

BH3

Glycolysis inhibition sensitizes tumor cells to death receptors-induced apoptosis by AMP kinase activation leading to Mcl-1 block in translation.
Pradelli LA, Bénéteau M, Chauvin C, Jacquin MA, Marchetti S, Muñoz-Pinedo C, Auberger P, Pende M, Ricci JE.
http://www.nature.com/onc/journal/vaop/ncurrent/full/onc2009448a.html

Caspase-independent Mitochondrial Cell Death Results from Loss of Respiration, Not Cytotoxic Protein Release
Lydia Lartigue, Yulia Kushnareva, Youngmo Seong, Helen Lin, Benjamin Faustin, and Donald D. Newmeyer
http://www.molbiolcell.org/cgi/content/abstract/20/23/4871?etoc

Single-cell quantification of Bax activation and mathematical modelling suggest pore formation on minimal mitochondrial Bax accumulation
HDüssmann, M Rehm, C G Concannon, S Anguissola, M Würstle, S Kacmar, P Völler, H J Huber and J H M Prehn
http://www.nature.com/cdd/journal/vaop/ncurrent/full/cdd2009123a.html

Functional Cooperation of the Proapoptotic Bcl2 Family Proteins Bmf and Bim In Vivo
Anette Hübner, Julie Cavanagh-Kyros, Mercedes Rincon, Richard A. Flavell, and Roger J. Davis
Mol. Cell. Biol. 2010;30 98-105
http://mcb.asm.org/cgi/content/abstract/30/1/98

Identification of proapoptotic Bim as a tumor suppressor in neoplastic mast cells: role of KIT D816V and effects of various targeted drugs
Karl J. Aichberger, Karoline V. Gleixner, Irina Mirkina, Sabine Cerny-Reiterer, Barbara Peter, Veronika Ferenc, Michael Kneidinger, Christian Baumgartner, Matthias Mayerhofer, Alexander Gruze, Winfried F. Pickl, Christian Sillaber, and Peter Valent
Blood 2009;114 5342-5351
http://bloodjournal.hematologylibrary.org/cgi/content/abstract/114/26/5342

VDAC2 is required for truncated BID-induced mitochondrial apoptosis by recruiting BAK to the mitochondria
Soumya Sinha Roy, Amy M Ehrlich, William J Craigen and György Hajnóczky
http://www.nature.com/embor/journal/v10/n12/abs/embor2009219.html

Voltage-dependent anion channel-1-based peptides interact with Bcl2 to prevent anti-apoptotic activity
Nir Arbel and Varda Shoshan-Barmatz
J. Biol. Chem. published 26 December 2009, 10.1074/jbc.M109.082990
http://www.jbc.org/cgi/content/abstract/M109.082990v1

Molecular details of Bax activation, oligomerization and membrane insertion
Stephanie Bleicken, Mirjam Classen, Pulagam V. L. Padmavathi, Takashi Ishikawa, Kornelius Zeth, Heinz-Jüergen Steinhoff, and Enrica Bordignon
J. Biol. Chem. published 13 December 2009, 10.1074/jbc.M109.081539
http://www.jbc.org/cgi/content/abstract/M109.081539v2

Vaccinia virus F1L interacts with Bak using highly divergent BCL-2 homology domains and replaces the function of Mcl-1
Stephanie Campbell, Bart Hazes, Marc Kvansakul, Peter Colman, and Michele Barry
J. Biol. Chem. published 2 December 2009, 10.1074/jbc.M109.053769
http://www.jbc.org/cgi/content/abstract/M109.053769v1

Bcl-xL changes conformation upon binding to wild-type but not mutant p53 DNA binding domain
Franz Hagn, Christian Klein, Oliver Demmer, Natasha Marchenko, Angelina Vaseva, Ute M. Moll, and Horst Kessler
J. Biol. Chem. published 2 December 2009, 10.1074/jbc.M109.065391
http://www.jbc.org/cgi/content/abstract/M109.065391v1
 

Death receptors and IAPs

Recruitment of the Linear Ubiquitin Chain Assembly Complex Stabilizes the TNF-R1 Signaling Complex and Is Required for TNF-Mediated Gene Induction
T.L. Haas, C.H. Emmerich, B. Gerlach, A.C. Schmukle, S.M. Cordier, E. Rieser, R. Feltham, J. Vince, U. Warnken, T. Wenger, R. Koschny, D. Komander, J. Silke, and H. Walczak
http://www.cell.com/molecular-cell/abstract/S1097-2765%2809%2900778-3

RIPK1 is not essential for TNFR1-induced activation of NF-B
W W-LWong, I E Gentle, U Nachbur, H Anderton, D L Vaux and J Silke
http://www.nature.com/cdd/journal/vaop/ncurrent/full/cdd2009178a.html

Cellular IAPs inhibit a cryptic CD95-induced cell death by limiting RIP1 kinase recruitment
Peter Geserick, Mike Hupe, Maryline Moulin, W. Wei-Lynn Wong, Maria Feoktistova, Beate Kellert, Harald Gollnick, John Silke, and Martin Leverkus
http://jcb.rupress.org/cgi/content/abstract/187/7/1037?etoc

Identification of an Xiap-Like Pseudogene on Mouse Chromosome 7
Aneta Kotevski, Wendy D. Cook, David L. Vaux, Bernard A. Callus
http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0008078

Modulation of Wnt signaling by the nuclear localization of cellular FLIP-L
Ryohei Katayama, Toshiyasu Ishioka, Shinji Takada, Ritsuko Takada, Naoya Fujita, Takashi Tsuruo, and Mikihiko Naito
J Cell Sci 2010;123 23-28
http://jcs.biologists.org/cgi/content/abstract/123/1/23

A Model of Partnership Co-Opted by the Homeodomain Protein TGIF and the Itch/AIP4 Ubiquitin Ligase for Effective Execution of TNF-α Cytotoxicity
C. Demange, N. Ferrand, C. Prunier, M.-F. Bourgeade, and A. Atfi
http://www.cell.com/molecular-cell/abstract/S1097-2765%2809%2900913-7
 

Caspases and downstream

Vaccinia Virus protein F1L is a caspase-9 inhibitor
Dayong Y. Zhai, Eric Yu, Chaofang Jin, Kate Welsh, Chung-wei Shiau, Lili Chen, Guy S. Salvesen, Robert Liddington, and John C. Reed
J. Biol. Chem. published 18 December 2009, 10.1074/jbc.M109.078113
http://www.jbc.org/cgi/content/abstract/M109.078113v1

Pretaporter, a Drosophila protein serving as a ligand for Draper in the phagocytosis of apoptotic cells
Takayuki Kuraishi, Yukiko Nakagawa, Kaz Nagaosa, Yumi Hashimoto, Takashi Ishimoto, Takeshi Moki, Yu Fujita, Hiroshi Nakayama, Naoshi Dohmae, Akiko Shiratsuchi, Naoko Yamamoto, Koichi Ueda, Masamitsu Yamaguchi, Takeshi Awasaki and Yoshinobu Nakanishi
http://www.nature.com/emboj/journal/v28/n24/abs/emboj2009343a.html

Annexin-II, DNA and histones serve as Factor H ligands on the surface of apoptotic cells
Jonatan Leffler, Andrew P. Herbert, Eva Norstrom, Chistoph Q. Schmidt, Paul N. Barlow, Anna M. Blom, and Myriam Martin
J. Biol. Chem. published 1 December 2009, 10.1074/jbc.M109.045427
http://www.jbc.org/cgi/content/abstract/M109.045427v1

 
Other

Inhibition of the ER Ca2+ pump forces multidrug-resistant cells deficient in Bak and Bax into necrosis
Katja Janssen, Sibylle Horn, Mathis T. Niemann, Peter T. Daniel, Klaus Schulze-Osthoff, and Ute Fischer
J Cell Sci 2009;122 4481-4491
http://jcs.biologists.org/cgi/content/abstract/122/24/4481

Yeast acetic acid-induced programmed cell death can occur without cytochrome c release which requires metacaspase YCA1
Nicoletta Guaragnella, Antonella Bobba, Salvatore Passarella, Ersilia Marra, Sergio Giannattasio
http://dx.doi.org/10.1016/j.febslet.2009.11.072
 
REVIEWS

A Tangled Web of Ubiquitin Chains: Breaking News in TNF-R1 Signaling
K. Bianchi and P. Meier
http://www.cell.com/molecular-cell/abstract/S1097-2765%2809%2900870-3

Mitochondrial cell death effectors
Dirk Brenner, Tak W Mak
http://dx.doi.org/10.1016/j.ceb.2009.09.009

Regulation of cell death by the ubiquitin–proteasome system
Maya Bader, Hermann Steller
http://dx.doi.org/10.1016/j.ceb.2009.09.005

Glucose metabolism and programmed cell death: an evolutionary and mechanistic perspective
Ayala King, Eyal Gottlieb
http://dx.doi.org/10.1016/j.ceb.2009.09.009

Caspase substrates: easily caught in deep waters?
Dieter Demon1, Petra Van Damme, Tom Vanden Berghe, Joël Vandekerckhove, Wim Declercq, Kris Gevaert and Peter Vandenabeele
http://dx.doi.org/10.1016/j.tibtech.2009.09.007

CDD: Special Issue on The Ubiquitin Proteasome System
http://www.nature.com/cdd/index.html

Including:

Regulation of TNFRSF and innate immune signalling complexes by TRAFs and cIAPs
J Silke and R Brink
http://www.nature.com/cdd/journal/v17/n1/full/cdd2009114a.html

The role of ubiquitylation for the control of cell death in Drosophila
A Bergmann
http://www.nature.com/cdd/journal/v17/n1/full/cdd200970a.html

 
COMMENTS

ER stress: another route to cell death
J Cell Sci 2009;122 e2401
http://jcs.biologists.org/cgi/content/full/122/24/e2401

Apoptosis: it’s BAK to VDAC
Gordon C. Shore
http://www.nature.com/embor/journal/v10/n12/full/embor2009249.html



Apolist – november 09

REVIEWS
.
Emerging Role for Members of the Bcl-2 Family in Mitochondrial Morphogenesis
A. Autret and S.J. Martin
http://dx.doi.org/10.1016/j.molcel.2009.10.011
.

Novel roles for GAPDH in cell death and carcinogenesis

A Colell, D R Green and J-E Ricci

.

Cell Death
Richard S. Hotchkiss, M.D., Andreas Strasser, Ph.D., Jonathan E.
McDunn, Ph.D., and Paul E. Swanson, M.D.
http://content.nejm.org/cgi/content/full/361/16/1570


BH3

Bak Activation for Apoptosis Involves Oligomerization of Dimers via
Their α6 Helices
G. Dewson, T. Kratina, P. Czabotar, C.L. Day, J.M. Adams, and R.M. Kluck
http://www.cell.com/molecular-cell/abstract/S1097-2765(09)00821-1

Membrane promotes tBID interaction with BCL(XL).
García-Sáez AJ, Ries J, Orzáez M, Pérez-Payà E, Schwille P.
http://www.nature.com/nsmb/journal/v16/n11/abs/nsmb.1671.html

Stepwise Activation of BAX and BAK by tBID, BIM, and PUMA Initiates
Mitochondrial Apoptosis
H. Kim, H.-C. Tu, D. Ren, O. Takeuchi, J.R. Jeffers, G.P. Zambetti,
J.J.-D. Hsieh, and E.H.-Y. Cheng
http://www.cell.com/molecular-cell/abstract/S1097-2765(09)00690-X

Bax contains two functional mitochondrial targeting sequences and
translocates to mitochondria in a conformational change- and
homo-oligomerization-driven process
Nicholas M. George, Natalie Targy, Jacquelynn J. D. Evans, Liqiang
Zhang, and Xu Luo
http://www.jbc.org/cgi/content/abstract/M109.049924v1

Bim Upregulation by Histone Deacetylase Inhibitors Mediates
Interactions with the Bcl-2 Antagonist ABT-737: Evidence for Distinct
Roles for Bcl-2, Bcl-xL, and Mcl-1
Shuang Chen, Yun Dai, Xin-Yan Pei, and Steven Grant
http://mcb.asm.org/cgi/content/abstract/29/23/6149

The BH3-only protein Bim plays a critical role in leukemia cell death
triggered by concomitant inhibition of the PI3K/Akt and MEK/ERK1/2
pathways
Mohamed Rahmani, Anh Anderson, Joseph Reza Habibi, Timothy Ryan
Crabtree, Mandy Mayo, Hisashi Harada, Andrea Ferreira-Gonzalez, Paul
Dent, and Steven Grant
http://bloodjournal.hematologylibrary.org/cgi/content/abstract/114/20/4507

From the Cover: Age-related hearing loss in C57BL/6J mice is mediated
by Bak-dependent mitochondrial apoptosis
Shinichi Someya, Jinze Xu, Kenji Kondo, Dalian Ding, Richard J. Salvi,
Tatsuya Yamasoba, Peter S. Rabinovitch, Richard Weindruch, Christiaan
Leeuwenburgh, Masaru Tanokura, and Tomas A. Prolla
http://www.pnas.org/content/106/46/19432.abstract?etoc

Facilitation of mitochondrial outer and inner membrane
permeabilization and cell death in oxidative stress by a novel BH3
domain protein
A. Szigeti, E. Hocsak, E. Rapolti, B. Racz, A. Boronkai, E. Pozsgai,
B. Debreceni, Z. Bognar, S. Bellyei, B. Sumegi, and F. Gallyas, Jr.
http://www.jbc.org/cgi/content/abstract/M109.015222v1

Dissimilar mechanisms of cytochrome c release induced by octyl
glucoside-activated BAX and by BAX activated with truncated BID
Tsyregma Li, Tatiana Brustovetsky, Bruno Antonsson, Nickolay Brustovetsky
http://dx.doi.org/10.1016/j.bbabio.2009.07.012


Miscellaneous

Autophagy, Not Apoptosis, Is Essential for Midgut Cell Death in Drosophila
D. Denton, B. Shravage, R. Simin, K. Mills, D.L. Berry, E.H.
Baehrecke, and S. Kumar
http://dx.doi.org/10.1016/j.cub.2009.08.042

Determinism and divergence of apoptosis susceptibility in mammalian cells
Patrick D. Bhola and Sanford M. Simon
J Cell Sci 2009;122 4296-4302
http://jcs.biologists.org/cgi/content/abstract/122/23/4296

GM1-Ganglioside Accumulation at the Mitochondria-Associated ER
Membranes Links ER Stress to Ca2+-Dependent Mitochondrial Apoptosis
R. Sano, I. Annunziata, A. Patterson, S. Moshiach, E. Gomero, J.
Opferman, M. Forte, and A. d’Azzo
http://www.cell.com/molecular-cell/abstract/S1097-2765(09)00786-2

Granzyme F induces a novel death pathway characterized by
Bid-independent cytochrome c release without caspase activation
LShi, L Wu, S Wang and Z Fan
http://www.nature.com/cdd/journal/v16/n12/abs/cdd2009101a.html


IAPs and death receptors

CD95 engagement mediates actin-independent and -dependent apoptotic signals
BChaigne-Delalande, W Mahfouf, S Daburon, J-F Moreau and P Legembre
http://www.nature.com/cdd/journal/v16/n12/abs/cdd2009111a.html

PU.1 induces apoptosis in myeloma cells through direct transactivation of TRAIL
S Ueno, H Tatetsu, H Hata, T Iino, H Niiro, K Akashi, D G Tenen, H
Mitsuya and Y Okuno
http://www.nature.com/onc/journal/v28/n46/full/onc2009263a.html

A role for X-linked inhibitor of apoptosis protein upstream of
mitochondrial permeabilization
Thomas W. Owens, Fiona M. Foster, Anthony Valentijn, Andrew P.
Gilmore, and Charles H. Streuli
http://www.jbc.org/cgi/content/abstract/M109.072322v1


Caspases and downstream

PPAR-δ senses and orchestrates clearance of apoptotic cells to promote tolerance

Lata Mukundan, Justin I Odegaard, Christine R Morel, Jose E Heredia, Julia W Mwangi, Roberto R Ricardo-Gonzalez, Y P Sharon Goh, Alex Red Eagle, Shannon E Dunn, Jennifer U H Awakuni, Khoa D Nguyen, Lawrence Steinman, Sara A Michie and Ajay Chawl

http://www.nature.com/nm/journal/v15/n11/full/nm.2048.html

Recognition of apoptotic cells by epithelial cells: conserved versus
tissue-specific signaling responses
Vimal A. Patel, Daniel J. Lee, Lanfei Feng, Angelika Antoni, Wilfred
Lieberthal, John H. Schwartz, Joyce Rauch, David S. Ucker, and Jerrold
S. Levine
J. Biol. Chem. published 12 November 2009, 10.1074/jbc.M109.018440
http://www.jbc.org/cgi/content/abstract/M109.018440v1

Necrotic cells trigger a sterile inflammatory response through the
Nlrp3 inflammasome
Shankar S. Iyer, Wilco P. Pulskens, Jeffrey J. Sadler, Loes M. Butter,
Gwendoline J. Teske, Tyler K. Ulland, Stephanie C. Eisenbarth,
Sandrine Florquin, Richard A. Flavell, Jaklien C. Leemans, and Fayyaz
S. Sutterwala
http://www.pnas.org/content/106/48/20388.abstract?etoc


COMMENTS

BAX and BAK Caught in the Act
Y. Yao and F.M. Marassi
http://www.cell.com/molecular-cell/abstract/S1097-2765(09)00788-6

Apoptosis: the generation gap
http://jcs.biologists.org/cgi/content/full/122/23/e2302?etoc

Caspase 2 in apoptosis, the DNA damage response and tumour
suppression: enigma no more?
Sharad Kumar
http://www.nature.com/nrc/journal/v9/n12/full/nrc2745.html

Apolist – october 2009

Caspases and downstream
————————————–

Temporal regulation of Drosophila IAP1 determines caspase functions in sensory organ development
Akiko Koto, Erina Kuranaga, and Masayuki Miura
http://jcb.rupress.org/cgi/content/abstract/187/2/219?etoc

Restraint of apoptosis during mitosis through interdomain phosphorylation of caspase-2
Joshua L Andersen, Carrie E Johnson, Christopher D Freel, Amanda B Parrish, Jennifer L Day, Marisa R Buchakjian, Leta K Nutt, J Will Thompson, M Arthur Moseley and Sally Kornbluth
http://www.nature.com/emboj/journal/v28/n20/abs/emboj2009253a.html

Conformational similarity in the activation of caspase-3 and -7 revealed by the unliganded and inhibited structures of caspase-7
Johnson Agniswamy, Bin Fang, Irene T. Weber
http://www.springerlink.com/content/37243830r711kw1u/

Continuous imaging of plasmon rulers in live cells reveals early-stage caspase-3 activation at the single-molecule level
Young-wook Jun, Sassan Sheikholeslami, Daniel R. Hostetter, Cheryl Tajon, Charles S. Craik, and A. Paul Alivisatos
http://www.pnas.org/content/106/42/17735.abstract

ARTEMIS Nuclease Facilitates Apoptotic Chromatin Cleavage
Sébastien Britton, Philippe Frit, Denis Biard, Bernard Salles, and Patrick Calsou
Cancer Res 2009;69 8120-8126
http://cancerres.aacrjournals.org/cgi/content/abstract/69/20/8120

Autophagy is not universally required for phosphatidyl-serine exposure and
apoptotic cell engulfment during neural development
María A. Mellén, Enrique J. de la Rosa and Patricia Boya
http://www.landesbioscience.com/journals/autophagy/article/9292

 

Death receptor pathway
———————————-

FLIP-mediated autophagy regulation in cell death control
Jong-Soo Lee, Qinglin Li, June-Yong Lee, Sun-Hwa Lee, Joseph H. Jeong, Hye-Ra Lee, Heesoon Chang, Fu-Chun Zhou, Shou-Jiang Gao, Chengyu Liang and Jae U. Jung
http://www.nature.com/ncb/journal/v11/n11/full/ncb1980.html

Down-regulation of c-FLIP Enhances Death of Cancer Cells by Smac Mimetic Compound
Herman H. Cheung, Douglas J. Mahoney, Eric C. LaCasse, and Robert G. Korneluk
http://cancerres.aacrjournals.org/cgi/content/abstract/69/19/7729

A Novel PTEN-Dependent Link to Ubiquitination Controls FLIPS Stability and TRAIL Sensitivity in Glioblastoma Multiforme
Amith Panner, Courtney A. Crane, Changjiang Weng, Alberto Feletti, Andrew T. Parsa, and Russell O. Pieper
http://cancerres.aacrjournals.org/cgi/content/abstract/69/20/7911

TRAF2 must bind to cIAPs for TNF to efficiently activate NF- B and to prevent TNF-induced apoptosis
James E. Vince, Delara Pantaki, Rebecca Feltham, Peter D. Mace, Stephanie M. Cordier, Anna C. Schmukle, Angelina J. Davidson, Bernard A. Callus, Wendy Wei-Lynn Wong, Ian E. Gentle, Holly Carter, Erinna F. Lee, Henning Walczak, Catherine L. Day, David L. Vaux, and John Silke
http://www.jbc.org/cgi/content/abstract/M109.072256v2

Down-regulation of RIP expression by 17-dimethylaminoethylamino-17-demethoxygeldanamycin promotes TRAIL-induced apoptosis in breast tumor cells.
Palacios C, López-Pérez AI, López-Rivas A.
http://dx.doi.org/10.1016/j.canlet.2009.06.012

XIAP regulates cell death induction by pro-apoptotic receptor agonists
Eugene Varfolomeev, Bruno Alicke, J. Michael Elliott, Kerry Zobel, Kristina West, Harvey Wong, Justin M. Scheer, Avi Ashkenazi, Stephen E. Gould, Wayne J. Fairbrother, and Domagoj Vucic
http://www.jbc.org/cgi/content/abstract/M109.040139v1

Plasmacytoid dendritic cells express TRAIL and induce CD4+ T-cell apoptosis in HIV-1 viremic patients
Georg Stary, Irene Klein, Sabine Kohlhofer, Frieder Koszik, Thomas Scherzer, Leonhard Müllauer, Heribert Quendler, Norbert Kohrgruber, and Georg Stingl
http://bloodjournal.hematologylibrary.org/cgi/content/abstract/114/18/3854

 

BH3
——-

Oligomerization of membrane-bound Bcl-2 is involved in its pore formation induced by tBid
Jun Peng, Jingzhen Ding, Chibing Tan, Bruce Baggenstoss, Zhi Zhang, Suzanne M. Lapolla, Jialing Lin
http://www.springerlink.com/content/u2g85655k10682j8/

MCL-1–dependent leukemia cells are more sensitive to chemotherapy than BCL-2–dependent counterparts
Joslyn K. Brunelle, Jeremy Ryan, Derek Yecies, Joseph T. Opferman, and Anthony Letai
http://jcb.rupress.org/cgi/content/abstract/187/3/429?etoc

Bax activates endophilin B1 oligomerization and lipid membrane vesiculation
Tatiana K. Rostovtseva, Hacene Boukari, Antonella Antignani, Brian Shiu, Soojay Banerjee, Albert Neutzner, and Richard J. Youle
http://www.jbc.org/cgi/content/abstract/M109.021873v1

Overactivation of the MEK/ERK Pathway in Liver Tumor Cells Confers Resistance to TGF-β–Induced Cell Death through Impairing Up-regulation of the NADPH Oxidase NOX4
Laia Caja, Patricia Sancho, Esther Bertran, Daniel Iglesias-Serret, Joan Gil, and Isabel Fabregat
http://cancerres.aacrjournals.org/cgi/content/abstract/69/19/7595

The anti-apoptotic molecule Bcl-2 regulates the differentiation, activation and survival of both osteoblasts and osteoclasts
Yuichi Nagase, Mitsuyasu Iwasawa, Toru Akiyama, Yuho Kadono, Masaki Nakamura, Yasushi Oshima, Tetsuro Yasui, Takumi Matsumoto, Jun Hirose, Hiroaki Nakamura, Takeshi Miyamoto, Philippe Bouillet, Kozo Nakamura, and Sakae Tanaka
http://www.jbc.org/cgi/content/abstract/M109.016915v1

Apoptosis commitment and activation of mitochondrial Bax during anoikis is regulated by p38MAPK
TW Owens, AJ Valentijn, J-P Upton, J Keeble, L Zhang, J Lindsay, NK Zouq and AP Gilmore
http://www.nature.com/cdd/journal/v16/n11/full/cdd2009102a.html

The Cell Death–Inducing Activity of the Peptide Containing Noxa Mitochondrial-Targeting Domain Is Associated with Calcium Release
Young-Woo Seo, Ha-Na Woo, Sujan Piya, Ae Ran Moon, Jae-Wook Oh, Cheol-Won Yun, Kyung-Keun Kim, Ji-Young Min, Seon-Yong Jeong, Seyung Chung, Peter I. Song, Seong-Yun Jeong, Eun Kyung Choi, Dai-Wu Seol, and Tae-Hyoung Kim
http://cancerres.aacrjournals.org/cgi/content/abstract/69/21/8356

Proteasome inhibitors induce apoptosis in human lung cancer cells through a positive feedback mechanism and the subsequent Mcl-1 protein cleavage
B-ZYuan, J Chapman and S H Reynolds
http://www.nature.com/onc/journal/v28/n43/abs/onc2009240a.html

 

Other
——–

Spatial and temporal dynamics of mitochondrial membrane permeability waves during apoptosis.
Bhola PD, Mattheyses AL, Simon SM.
http://dx.doi.org/10.1016/j.bpj.2009.07.056

Polypyrimidine tract binding proteins (PTB) regulate the expression of apoptotic genes and susceptibility to caspase-dependent apoptosis in differentiating cardiomyocytes
J Zhang, N Bahi, M Llovera, J X Comella and D Sanchis
http://www.nature.com/cdd/journal/v16/n11/full/cdd200987a.html

A novel membrane fusion-mediated plant immunity against bacterial pathogens
Noriyuki Hatsugai, Shinji Iwasaki, Kentaro Tamura, Maki Kondo, Kentaro Fuji, Kimi Ogasawara, Mikio Nishimura, and Ikuko Hara-Nishimura
http://genesdev.cshlp.org/cgi/content/abstract/23/21/2496

 

REVIEWS / COMMENTS
————————————–

Apoptosis: Calling Time on Apoptosome Activity
Colin Adrain and Seamus J. Martin
Caspase-9 autoprocessing displaces active caspase-9 bound to the apoptosome, thereby limiting proteolytic activity.
http://stke.sciencemag.org/cgi/content/abstract/sigtrans;2/91/pe62?etoc

Apoptosis: Watching caspase 2 get active
Katharine H. Wrighton
http://www.nature.com/nrm/journal/v10/n11/full/nrm2788.html

Walking a fine caspase line
Kendall Powell
http://jcb.rupress.org/cgi/content/full/187/2/150?etoc

HIV infection: TRAILing the killers
Andrea Cerutti
http://bloodjournal.hematologylibrary.org/cgi/content/full/114/18/3723

A kiss of death—proteasome-mediated membrane fusion and programmed cell death in plant defense against bacterial infection
Karolina Pajerowska-Mukhtar and Xinnian Dong
http://genesdev.cshlp.org/cgi/content/abstract/23/21/2449