Apolist – july 2009

Death receptors and IAPs

XIAP discriminates between type I and type II FAS-induced apoptosis
Philipp J. Jost, Stephanie Grabow1,2, Daniel Gray1, Mark D. McKenzie2,3, Ueli Nachbur4, David C. S. Huang1, Philippe Bouillet, Helen E. Thomas3, Christoph Borner, John Silke, Andreas Strasser & Thomas Kaufmann1
http://www.nature.com/nature/journal/vaop/ncurrent/full/nature08229.html#B19
PMID 19626005

RIP3, an Energy Metabolism Regulator That Switches TNF-Induced Cell Death from Apoptosis to Necrosis
D.-W. Zhang et al.
http://www.sciencemag.org/cgi/content/abstract/325/5938/332
PMID 19498109

A single nucleotide polymorphism determines protein isoform production of the human c-FLIP protein
Nana Ueffing, Kusum K. Singh, Andrea Christians, Christoph Thorns, Alfred C. Feller, Florian Nagl, Falko Fend, Sebastian Heikaus, Alexander Marx, Rainer B. Zotz, Joachim Brade, Wolfgang A. Schulz, Klaus Schulze-Osthoff, Ingo Schmitz, and Christian Schwerk
http://bloodjournal.hematologylibrary.org/cgi/content/abstract/114/3/572

X-linked Inhibitor of Apoptosis Protein (XIAP) Regulates PTEN Ubiquitination, Content, and Compartmentalization
Céline Van Themsche, Valérie Leblanc, Sophie Parent, and Eric Asselin
http://www.jbc.org/cgi/content/abstract/284/31/20462

—
Caspases

Suppression of Interleukin-33 Bioactivity through Proteolysis by Apoptotic Caspases
Alexander U. Lüthi, Sean P. Cullen, Edel A. McNeela, Patrick J. Duriez, Inna S. Afonina, Clare Sheridan, Gabriela Brumatti, Rebecca C. Taylor, Kristof Kersse, Peter Vandenabeele, Ed C. Lavelle, Seamus J. Martin
http://www.cell.com/immunity/abstract/S1074-7613(09)00269-6

The Apaf-1-procaspase-9 apoptosome complex functions as a proteolytic-based molecular timer
Srinivas Malladi, Madhavi Challa-Malladi, Howard O Fearnhead and Shawn B Bratton
http://www.nature.com/emboj/journal/v28/n13/full/emboj2009152a.html

Dissecting an allosteric switch in caspase-7 using chemical and mutational probes
Jeanne A. Hardy and James A. Wells
http://www.jbc.org/cgi/content/abstract/M109.001826v1

Calpain-1 cleaves and activates caspase-7
Juliette Gafni, Xin Cong, Sylvia F. Chen, Bradford W. Gibson, and Lisa M. Ellerby
http://www.jbc.org/cgi/content/abstract/M109.038174v2

Genetic variation in caspase genes and risk of non-Hodgkin lymphoma: a pooled analysis of 3 population-based case-control studies
Qing Lan, Lindsay M. Morton, Bruce Armstrong2, Patricia Hartge1, Idan Menashe1, Tongzhang Zheng3, Mark P. Purdue1, James R. Cerhan4, Yawei Zhang3, Andrew Grulich5, Wendy Cozen6, Meredith Yeager7, Theodore R. Holford3, Claire M. Vajdic8, Scott Davis9, Brian Leaderer3, Anne Kricker2, Maryjean Schenk10, Shelia H. Zahm1, Nilanjan Chatterjee1, Stephen J. Chanock1,7, Nathaniel Rothman1, and Sophia S. Wang
http://bloodjournal.hematologylibrary.org/cgi/content/abstract/114/2/264?etoc

—
BH3

PUMA Promotes Bax Translocation by Both Directly Interacting with Bax and by Competitive Binding to Bcl-XL during UV-induced Apoptosis
Yingjie Zhang, Da Xing, and Lei Liu
http://www.molbiolcell.org/cgi/content/abstract/20/13/3077?etoc

Detergent activated BAX protein is a monomer
Olena Ivashyna, Ana J. Garcia-Saez, Jonas Ries, Eric T. Christenson, Petra Schwille, and Paul H. Schlesinger
http://www.jbc.org/cgi/content/abstract/M109.023853v1

PUMA- and Bax-induced autophagy contributes to apoptosis
K S Yee, S Wilkinson, J James, K M Ryan & K H Vousden
http://www.nature.com/cdd/journal/v16/n8/full/cdd200944a.html

MAP4K3 modulates cell death via the post-transcriptional regulation of BH3-only proteins
David Lam, David Dickens, Elizabeth B. Reid, Samantha H. Y. Loh, Nicoleta Moisoi, and L. Miguel Martins
http://www.pnas.org/content/106/29/11978.abstract?etoc

—
Other

MDM4 (MDMX) localizes at the mitochondria and facilitates the p53-mediated intrinsic-apoptotic pathway
Francesca Mancini, Giusy Di Conza, Marsha Pellegrino, Cinzia Rinaldo, Andrea Prodosmo, Simona Giglio, Igea D’Agnano, Fulvio Florenzano, Lara Felicioni, Fiamma Buttitta, Antonio Marchetti, Ada Sacchi, Alfredo Pontecorvi, Silvia Soddu and Fabiola Moretti
http://www.nature.com/emboj/journal/v28/n13/full/emboj2009154a.html

A novel role for MAP1 LC3 in nonautophagic cytoplasmic vacuolation death of cancer cells
R Kar, P K Singha, M A Venkatachalam & P Saikumar
http://www.nature.com/onc/journal/v28/n28/full/onc2009118a.html

—
REVIEWS / COMMENTS

Guidelines for the use and interpretation of assays for monitoring cell death in higher eukaryotes
(plenty of authors)
http://www.nature.com/cdd/journal/v16/n8/full/cdd200944a.html

BCL2DB: moving ‘helix-bundled’ BCL-2 family members to their database
Stanislas Valentin Blaineau, Abdel Aouacheria
http://www.springerlink.com/content/j6x5l4117x50ph7m/

IL-33 Raises Alarm
M. Lamkanfi and V.M. Dixit
http://www.cell.com/immunity/abstract/S1074-7613(09)00284-2

Mitochondrial targeting of tBid/Bax: a role for the TOM complex?
M Ott, E Norberg, B Zhivotovsky & S Orrenius
http://www.nature.com/cdd/journal/v16/n8/full/cdd200961a.html

Caspase-8 for Outer Harmony
Gabriel Sollberger and Hans-Dietmar Beer
http://stke.sciencemag.org/cgi/content/abstract/sigtrans;2/78/pe40?etoc

Caspase-2: controversial killer or checkpoint controller?
Tanja Kitevska, Damian M. S. Spencer, Christine J. Hawkins
http://www.springerlink.com/content/q88h871q37540753/

Death receptors and IAPs

XIAP discriminates between type I and type II FAS-induced apoptosis

Philipp J. Jost, Stephanie Grabow1,2, Daniel Gray1, Mark D. McKenzie2,3, Ueli Nachbur4, David C. S. Huang1, Philippe Bouillet, Helen E. Thomas3, Christoph Borner, John Silke, Andreas Strasser & Thomas Kaufmann1

http://www.nature.com/nature/journal/vaop/ncurrent/full/nature08229.html#B19

PMID 19626005

RIP3, an Energy Metabolism Regulator That Switches TNF-Induced Cell Death from Apoptosis to Necrosis

D.-W. Zhang et al.

http://www.sciencemag.org/cgi/content/abstract/325/5938/332

PMID 19498109

A single nucleotide polymorphism determines protein isoform production of the human c-FLIP protein

Nana Ueffing, Kusum K. Singh, Andrea Christians, Christoph Thorns, Alfred C. Feller, Florian Nagl, Falko Fend, Sebastian Heikaus, Alexander Marx, Rainer B. Zotz, Joachim Brade, Wolfgang A. Schulz, Klaus Schulze-Osthoff, Ingo Schmitz, and Christian Schwerk

http://bloodjournal.hematologylibrary.org/cgi/content/abstract/114/3/572

X-linked Inhibitor of Apoptosis Protein (XIAP) Regulates PTEN Ubiquitination, Content, and Compartmentalization

Céline Van Themsche, Valérie Leblanc, Sophie Parent, and Eric Asselin

http://www.jbc.org/cgi/content/abstract/284/31/20462

Caspases

Suppression of Interleukin-33 Bioactivity through Proteolysis by Apoptotic Caspases

Alexander U. Lüthi, Sean P. Cullen, Edel A. McNeela, Patrick J. Duriez, Inna S. Afonina, Clare Sheridan, Gabriela Brumatti, Rebecca C. Taylor, Kristof Kersse, Peter Vandenabeele, Ed C. Lavelle, Seamus J. Martin

http://www.cell.com/immunity/abstract/S1074-7613(09)00269-6

The Apaf-1-procaspase-9 apoptosome complex functions as a proteolytic-based molecular timer

Srinivas Malladi, Madhavi Challa-Malladi, Howard O Fearnhead and Shawn B Bratton

http://www.nature.com/emboj/journal/v28/n13/full/emboj2009152a.html

Dissecting an allosteric switch in caspase-7 using chemical and mutational probes

Jeanne A. Hardy and James A. Wells

http://www.jbc.org/cgi/content/abstract/M109.001826v1

Calpain-1 cleaves and activates caspase-7

Juliette Gafni, Xin Cong, Sylvia F. Chen, Bradford W. Gibson, and Lisa M. Ellerby

http://www.jbc.org/cgi/content/abstract/M109.038174v2

Genetic variation in caspase genes and risk of non-Hodgkin lymphoma: a pooled analysis of 3 population-based case-control studies

Qing Lan, Lindsay M. Morton, Bruce Armstrong2, Patricia Hartge1, Idan Menashe1, Tongzhang Zheng3, Mark P. Purdue1, James R. Cerhan4, Yawei Zhang3, Andrew Grulich5, Wendy Cozen6, Meredith Yeager7, Theodore R. Holford3, Claire M. Vajdic8, Scott Davis9, Brian Leaderer3, Anne Kricker2, Maryjean Schenk10, Shelia H. Zahm1, Nilanjan Chatterjee1, Stephen J. Chanock1,7, Nathaniel Rothman1, and Sophia S. Wang

http://bloodjournal.hematologylibrary.org/cgi/content/abstract/114/2/264?etoc

BH3

PUMA Promotes Bax Translocation by Both Directly Interacting with Bax and by Competitive Binding to Bcl-XL during UV-induced Apoptosis

Yingjie Zhang, Da Xing, and Lei Liu

http://www.molbiolcell.org/cgi/content/abstract/20/13/3077?etoc

Detergent activated BAX protein is a monomer

Olena Ivashyna, Ana J. Garcia-Saez, Jonas Ries, Eric T. Christenson, Petra Schwille, and Paul H. Schlesinger

http://www.jbc.org/cgi/content/abstract/M109.023853v1

PUMA- and Bax-induced autophagy contributes to apoptosis

K S Yee, S Wilkinson, J James, K M Ryan & K H Vousden

http://www.nature.com/cdd/journal/v16/n8/full/cdd200944a.html

MAP4K3 modulates cell death via the post-transcriptional regulation of BH3-only proteins

David Lam, David Dickens, Elizabeth B. Reid, Samantha H. Y. Loh, Nicoleta Moisoi, and L. Miguel Martins

http://www.pnas.org/content/106/29/11978.abstract?etoc

Other

MDM4 (MDMX) localizes at the mitochondria and facilitates the p53-mediated intrinsic-apoptotic pathway

Francesca Mancini, Giusy Di Conza, Marsha Pellegrino, Cinzia Rinaldo, Andrea Prodosmo, Simona Giglio, Igea D’Agnano, Fulvio Florenzano, Lara Felicioni, Fiamma Buttitta, Antonio Marchetti, Ada Sacchi, Alfredo Pontecorvi, Silvia Soddu and Fabiola Moretti

http://www.nature.com/emboj/journal/v28/n13/full/emboj2009154a.html

A novel role for MAP1 LC3 in nonautophagic cytoplasmic vacuolation death of cancer cells

R Kar, P K Singha, M A Venkatachalam & P Saikumar

http://www.nature.com/onc/journal/v28/n28/full/onc2009118a.html

REVIEWS / COMMENTS

Guidelines for the use and interpretation of assays for monitoring cell death in higher eukaryotes

(plenty of authors)

http://www.nature.com/cdd/journal/v16/n8/full/cdd200944a.html

BCL2DB: moving ‘helix-bundled’ BCL-2 family members to their database

Stanislas Valentin Blaineau, Abdel Aouacheria

http://www.springerlink.com/content/j6x5l4117x50ph7m/

IL-33 Raises Alarm

M. Lamkanfi and V.M. Dixit

http://www.cell.com/immunity/abstract/S1074-7613(09)00284-2

Mitochondrial targeting of tBid/Bax: a role for the TOM complex?

M Ott, E Norberg, B Zhivotovsky & S Orrenius

http://www.nature.com/cdd/journal/v16/n8/full/cdd200961a.html

Caspase-8 for Outer Harmony

Gabriel Sollberger and Hans-Dietmar Beer

http://stke.sciencemag.org/cgi/content/abstract/sigtrans;2/78/pe40?etoc

Caspase-2: controversial killer or checkpoint controller?

Tanja Kitevska, Damian M. S. Spencer, Christine J. Hawkins

http://www.springerlink.com/content/q88h871q37540753/

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Apolist – june 2009

Genome-wide silencing in Drosophila captures conserved apoptotic effectors
Su Kit Chew et al.
http://www.nature.com/nature/journal/vaop/ncurrent/full/nature08087.html

—
Death receptors and IAPs

Receptor Interacting Protein Kinase-3 Determines Cellular Necrotic Response to TNF-α
S. He, L. Wang, L. Miao, T. Wang, F. Du, L. Zhao, and X. Wang
http://www.cell.com/abstract/S0092-8674%2809%2900578-9

Phosphorylation-Driven Assembly of the RIP1-RIP3 Complex Regulates Programmed Necrosis and Virus-Induced Inflammation
Y.S. Cho, S. Challa, D. Moquin, R. Genga, T.D. Ray, M. Guildford, and F.K.-M. Chan
http://www.cell.com/abstract/S0092-8674%2809%2900642-4

Phenylarsine oxide interferes with the death inducing signaling complex and inhibits tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) induced apoptosis.
Sun XM, Canda-Sánchez A, Manjeri GR, Cohen GM, Pinkoski MJ.
http://dx.doi.org/10.1016/j.yexcr.2009.05.014

TAK1 kinase determines TRAIL sensitivity by modulating reactive oxygen species and cIAP
S Morioka, E Omori, T Kajino, R Kajino-Sakamoto, K Matsumoto & J Ninomiya-Tsuji
http://www.nature.com/onc/journal/v28/n23/full/onc2009110a.html

CD95 co-stimulation blocks activation of naive T cells by inhibiting T cell receptor signaling
Gudrun Strauss, Jonathan A. Lindquist, Nathalie Arhel, Edward Felder, Sabine Karl, Tobias L. Haas, Simone Fulda, Henning Walczak, Frank Kirchhoff, and Klaus-Michael Debatin
http://jem.rupress.org/cgi/content/abstract/206/6/1379?etoc

Cytotoxicity mediated by the FASL-activated apoptotic pathway in stem cells
Julia Mazar, Molly Thomas, Ludmila Bezrukov, Alexander Chanturia, Gulcin Pekkurnaz, Shurong Yin, Sergei A. Kuznetsov, Pamela Gehron Robey, and Joshua Zimmerberg
http://www.jbc.org/cgi/content/abstract/M109.032235v1

—
BH3

Mitochondrial apoptosis induced by BH3-only molecules in the exclusive presence of endoplasmic reticular Bak
Martina Klee, Kathrin Pallauf, Sonia Alcalá, Aarne Fleischer and Felipe X Pimentel-Muiños
http://www.nature.com/emboj/journal/v28/n12/abs/emboj200990a.html

KLF6-SV1 Is a Novel Antiapoptotic Protein That Targets the BH3-Only Protein NOXA for Degradation and Whose Inhibition Extends Survival in an Ovarian Cancer Model
Analisa DiFeo, Fei Huang, Jaya Sangodkar, Esteban A. Terzo, Devin Leake, Goutham Narla, and John A. Martignetti
http://cancerres.aacrjournals.org/cgi/content/abstract/69/11/4733

Acetylation of the DNA binding domain regulates transcription-independent apoptosis by p53
Stephen M. Sykes, Timothy J. Stanek, Amanda Frank, Maureen E. Murphy, and Steven B. McMahon
http://www.jbc.org/cgi/content/abstract/M109.026096v1

BimL directly neutralizes Bcl-xL to promote Bax activation during UV-induced apoptosis
Xianwang Wang, Da Xing, Lei Liu, Wei R. Chen
http://dx.doi.org/10.1016/j.febslet.2009.04.045

PUMA Suppresses Intestinal Tumorigenesis in Mice
Wei Qiu, Eleanor B. Carson-Walter, Shih Fan Kuan, Lin Zhang, and Jian Yu
http://cancerres.aacrjournals.org/cgi/content/abstract/69/12/4999

PUMA mediates EGFR tyrosine kinase inhibitor-induced apoptosis in head and neck cancer cells
Q Sun, L Ming, S M Thomas, Y Wang, Z G Chen, R L Ferris, J R Grandis, L Zhang & J Yu
http://www.nature.com/onc/journal/v28/n24/full/onc2009108a.html

Different forms of cell death induced by putative BCL2 inhibitors
M Vogler, K Weber, D Dinsdale, I Schmitz, K Schulze-Osthoff, M J S Dyer & G M Cohen
http://www.nature.com/cdd/journal/v16/n7/full/cdd200948a.html

Mcl-1 Integrates the Opposing Actions of Signaling Pathways That Mediate Survival and Apoptosis
Caroline Morel, Scott M. Carlson, Forest M. White, and Roger J. Davis
http://mcb.asm.org/cgi/content/abstract/29/14/3845

Adenine Nucleotide Translocator Cooperates with Core Cell Death Machinery To Promote Apoptosis in Caenorhabditis elegans
Qinfang Shen, Fengsong Qin, Zhiyang Gao, Jie Cui, Hui Xiao, Zhiheng Xu, and Chonglin Yang
http://mcb.asm.org/cgi/content/abstract/29/14/3881

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IAPs, caspases and downstream

Cellular Inhibitors of Apoptosis cIAP1 and cIAP2 Are Required for Innate Immunity Signaling by the Pattern Recognition Receptors NOD1 and NOD2
M.J.M. Bertrand, K. Doiron, K. Labb_e, R.G. Korneluk, P.A. Barker, and M. Saleh
http://dx.doi.org/10.1016/j.immuni.2009.04.011

Gender differences in expression of the human caspase-12 long variant determines susceptibility to Listeria monocytogenes infection
Garabet Yeretssian, Karine Doiron, Wei Shao, Blair R. Leavitt, Michael R. Hayden, Donald W. Nicholson, and Maya Saleh
http://www.pnas.org/cgi/content/abstract/106/22/9016?etoc

Enhanced cytoprotective effects of the IAP protein, c-IAP1, through stabilization with TRAF2
Rebecca A. Csomos, Graham F. Brady, and Colin S. Duckett
http://www.jbc.org/cgi/content/abstract/M109.029983v1

Critical Role for Caspase-8 in Epidermal Growth Factor Signaling
Darren Finlay, Amy Howes, and Kristiina Vuori
http://cancerres.aacrjournals.org/cgi/content/abstract/69/12/5023

Caspase-10-Mediated Heat Shock Protein 90β Cleavage Promotes UVB Irradiation-Induced Cell Apoptosis
Hehua Chen, Yan Xia, Dexing Fang, David Hawke, and Zhimin Lu
http://mcb.asm.org/cgi/content/abstract/29/13/3657

Ordering of caspases in cells undergoing apoptosis by the intrinsic pathway
S Inoue, G Browne, G Melino & G M Cohen
http://www.nature.com/cdd/journal/v16/n7/full/cdd200929a.html

Single-cell imaging of retinal ganglion cell apoptosis with a cell-penetrating, activatable peptide probe in an in vivo glaucoma model
Edward M. Barnett, Xu Zhang, Dustin Maxwell, Qing Chang, and David Piwnica-Worms
http://www.pnas.org/content/106/23/9391.abstract?etoc

The antiapoptotic protein AAC-11 interacts with and regulates Acinus-mediated DNA fragmentation
Patricia Rigou, Valeria Piddubnyak, Audrey Faye, Jean-Christophe Rain, Laurence Michel, Fabien Calvo and Jean-Luc Poyet
http://www.nature.com/emboj/journal/v28/n11/abs/emboj2009106a.html
—

REVIEWS / COMMENTS

A few reviews on autophagy in CDD: http://www.nature.com/cdd/journal/v16/n7/index.html

Caspase activation pathways: some recent progress
S P Cullen & S J Martin
http://www.nature.com/cdd/journal/v16/n7/full/cdd200959a.html

Dynamics of mitochondrial structure during apoptosis and the enigma of Opa1
Ryuji Yamaguchi, Guy Perkins
http://dx.doi.org/10.1016/j.bbabio.2009.02.005

cIAP Proteins: Keystones in NOD Receptor Signal Transduction
C. Reardon and T.W. Mak
http://www.cell.com/immunity/abstract/S1074-7613%2809%2900243-X

Targeting Bcl-2 based on the interaction of its BH4 domain with the inositol 1,4,5-trisphosphate receptor
Yi-Ping Rong, Paul Barr, Vivien C. Yee, Clark W. Distelhorst http://www.sciencedirect.com/science/journal/01674889

Letting go: modification of cell adhesion during apoptosis
Suzanne M, Steller H
http://jbiol.com/content/8/5/49

When separation means death: killing through the mitochondria, but starting from the endoplasmic reticulum
Violeta Lamarca and Luca Scorrano
http://www.nature.com/emboj/journal/v28/n12/full/emboj2009135a.html

Apoptosis: Death by ubiquitylation
http://www.nature.com/nrm/journal/v10/n7/full/nrm2714.html

Apoptosis and cancer: the genesis of a research field
Thomas G. Cotter
http://www.nature.com/nrc/journal/v9/n7/full/nrc2663.html

Supplemental Siberia I – into the cold
Mole
http://jcs.biologists.org/cgi/content/full/122/12/1931
Supplemental material: http://jcs.biologists.org/cgi/content/full/122/12/1931/DC1