Apoptosis and cell death

Apolist: monthly literature updates for researchers

Archive for April, 2012

Apolist – April 2012

Posted by cris on April 30, 2012

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Bcl-2 family
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Mitochondrial pathway of apoptosis is ancestral in metazoans
Cheryl E. Bender, Patrick Fitzgerald, Stephen W. G. Tait, Fabien Llambi, Gavin P. McStay, Douglas O. Tupper, Jason Pellettieri, Alejandro Sánchez Alvarado, Guy S. Salvesen, and Douglas R. Green
http://www.pnas.org/content/109/13/4904.full

BH3-only proteins are part of a regulatory network that control the sustained signalling of the unfolded protein response sensor IRE1α
Rodriguez DA, Zamorano S, Lisbona F, Rojas-Rivera D, Urra H, Cubillos-Ruiz JR, Armisen R, Henriquez DR, H Cheng E, Letek M, Vaisar T, Irrazabal T,Gonzalez-Billault C, Letai A, Pimentel-Muiños FX, Kroemer G, Hetz C.
http://www.nature.com/emboj/journal/vaop/ncurrent/full/emboj201284a.html

Nigericin-induced impairment of autophagic flux in neuronal cells is inhibited by overexpression of Bak
Junghyun Lim, Yunsu Lee, Hyun-Wook Kim, Im Joo Rhyu, Myung Sook Oh, Moussa B. H. Youdim, Zhenyu Yue, and Young J. Oh
http://www.jbc.org/cgi/content/abstract/M112.364281v1

Downregulation of BCL2 by miRNAs augments drug-induced apoptosis – a combined computational and experimental approach
Richa Singh and Neeru Saini
http://jcs.biologists.org/cgi/content/abstract/125/6/1568

Inhibition of Mcl-1 Promotes Senescence in Cancer Cells: Implications for Preventing Tumor Growth and Chemotherapy Resistance
Elzbieta Bolesta, Lukas W. Pfannenstiel, Abeba Demelash, Mathew L. Lesniewski, Megan Tobin, Simon E. Schlanger, Shreeram C. Nallar, John C. Papadimitriou, Dhan V. Kalvakolanu, and Brian R. Gastman
http://mcb.asm.org/cgi/content/abstract/32/10/1879

Bax regulates primary necrosis through mitochondrial dynamics
Russell S. Whelan, Klitos Konstantinidis, An-Chi Wei, Yun Chen, Denis E. Reyna, Saurabh Jha, Ying Yang, John W. Calvert, Tullia Lindsten, Craig B. Thompson, Michael T. Crow, Evripidis Gavathiotis, Gerald W. Dorn, II, Brian O’Rourke, and Richard N. Kitsis
http://www.pnas.org/content/109/17/6566.abstract?etoc

FOXO3-induced reactive oxygen species are regulated by BCL2L11 (Bim) and SESN3
Judith Hagenbuchner, Andrey Kuznetsov, Martin Hermann, Barbara Hausott, Petra Obexer, and Michael J. Ausserlechner
http://jcs.biologists.org/cgi/content/abstract/125/5/1191

Chemical Genomics Identifies Small-Molecule MCL1 Repressors and BCL-xL as a Predictor of MCL1 Dependency
Guo Wei, Adam A. Margolin, Leila Haery, Emily Brown, Lisa Cucolo, Bina Julian, Shyemaa Shehata, Andrew L. Kung, Rameen Beroukhim, Todd R. Golub
http://www.cell.com/cancer-cell/abstract/S1535-6108%2812%2900126-2

The Bcl-2 proteins Noxa and Bcl-xL co-ordinately regulate oxidative stress-induced apoptosis
Colins O. Eno, Guoping Zhao, Kristen E. Olberding and Chi Li
http://www.biochemj.org/bj/444/bj4440069.htm

The Trim39 ubiquitin ligase inhibits APC/CCdh1-mediated degradation of the Bax activator MOAP-1
Nai-Jia Huang, Liguo Zhang, Wanli Tang, Chen Chen, Chih-Sheng Yang, and Sally Kornbluth
http://jcb.rupress.org/cgi/content/abstract/197/3/361?etoc

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Caspases and IAPs
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An inactivating caspase 11 passenger mutation originating from the 129 murine strain in mice targeted for c-IAP1
Niall S. Kenneth, J. Michael Younger, Elizabeth D. Hughes, Danielle Marcotte, Philip A. Barker, Thomas L. Saunders and Colin S. Duckett
http://www.biochemj.org/bj/443/bj4430355.htm

Caspase-7 uses an exosite to promote poly(ADP ribose) polymerase 1 proteolysis
Dave Boucher, Véronique Blais, and Jean-Bernard Denault
http://www.pnas.org/content/109/15/5669.abstract?etoc

Cathepsin D primes caspase-8 activation by multiple intra-chain proteolysis
Sébastien Conus, Cristina Pop, Scott J. Snipas, Guy S. Salvesen, and Hans-Uwe Simon
http://www.jbc.org/cgi/content/abstract/M111.306399v1

Phosphorylation regulates assembly of the caspase-6 substrate-binding groove.
Velázquez-Delgado EM, Hardy JA.
http://www.cell.com/structure/retrieve/pii/S0969212612000597

IAPs limit activation of RIP kinases by TNF receptor 1 during development
Maryline Moulin, Holly Anderton, Anne K Voss, Tim Thomas, Wendy Wei-Lynn Wong, Aleksandra Bankovacki, Rebecca Feltham, Diep Chau, Wendy D Cook, John Silke and David L Vaux
http://www.nature.com/emboj/journal/v31/n7/abs/emboj201218a.html

Caspase-8 is essential for maintaining chromosomal stability and suppressing B-cell lymphomagenesis
Anne Hakem, Samah El Ghamrasni, Georges Maire, Benedicte Lemmers, Jana Karaskova, Andrea Jurisicova, Otto Sanchez, Jeremy Squire, and Razqallah Hakem
http://bloodjournal.hematologylibrary.org/cgi/content/abstract/119/15/3495

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Death receptors
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Mixed lineage kinase domain-like is a key receptor interacting protein 3 downstream component of TNF-induced necrosis
Jie Zhao, Siriporn Jitkaew, Zhenyu Cai, Swati Choksi, Qiuning Li, Ji Luo, and Zheng-Gang Liu
http://www.pnas.org/content/109/14/5322.abstract?etoc

ER stress sensitizes cells to TRAIL through down-regulation of FLIP and Mcl-1 and PERK-dependent up-regulation of TRAIL-R2
Rosa Martín-Pérez, Maho Niwa and Abelardo López-Rivas
http://www.springerlink.com/content/30776359025287v2/

Caspase-3 feeds back on caspase-8, Bid and XIAP in type I Fas signaling in primary mouse hepatocytes
Karine Sá Ferreira, Clemens Kreutz, Sabine MacNelly, Karin Neubert, Angelika Haber, Matthew Bogyo, Jens Timmer & Christoph Borner
http://www.springerlink.com/content/m122541jn5q70333/

In mouse embryonic fibroblasts, neither caspase-8 nor cellular FLICE-inhibitory protein (FLIP) is necessary for TNF to activate NF-κB, but caspase-8 is required for TNF to cause cell death, and induction of FLIP by NF-κB is required to prevent it
D M Moujalled, W D Cook, J M Lluis, N R Khan, A U Ahmed, B A Callus and D L Vaux
http://www.nature.com/cdd/journal/v19/n5/abs/cdd2011151a.html

De-ubiquitinating protease USP2a targets RIP1 and TRAF2 to mediate cell death by TNF
A-L Mahul-Mellier, E Pazarentzos, C Datler, R Iwasawa, G AbuAli, B Lin and S Grimm
http://www.nature.com/cdd/journal/v19/n5/abs/cdd2011185a.html

Superior antitumoral activity of dimerized targeted single-chain TRAIL fusion proteins under retention of tumor selectivity
M Siegemund, N Pollak, O Seifert, K Wahl, K Hanak, A Vogel, A K Nussler, D Göttsch, S Münkel, H Bantel, R E Kontermann and K Pfizenmaier
http://www.nature.com/cddis/journal/v3/n4/abs/cddis201229a.html

Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) induces Death Receptor 5 networks that are highly organized
Christopher C. Valley, Andrew K. Lewis, Deepti J. Mudaliar, Jason D. Perlmutter, Anthony R. Braun, Christine B. Karim, David D. Thomas, Jonathan R. Brody, and Jonathan N. Sachs
http://www.jbc.org/cgi/content/abstract/M111.306480v1

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Miscellaneous
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Cdc6 protein obstructs apoptosome assembly and consequent cell death by forming stable complexes with activated Apaf-1 molecules
Shinichiro Niimi, Shiho Arakawa-Takeuchi, Baasanjav Uranbileg, Jun-ha Park, Shigeki Jinno, and Hiroto Okayama
http://www.jbc.org/cgi/content/abstract/M112.347690v1

Tumor Suppressor PDCD4 Represses Internal Ribosome Entry Site-Mediated Translation of Antiapoptotic Proteins and Is Regulated by S6 Kinase 2
Urszula Liwak, Nehal Thakor, Lindsay E. Jordan, Rajat Roy, Stephen M. Lewis, Olivier E. Pardo, Michael Seckl, and Martin Holcik
http://mcb.asm.org/cgi/content/abstract/32/10/1818

Autophagy genes function sequentially to promote apoptotic cell corpse degradation in the engulfing cell
Wei Li, Wei Zou, Yihong Yang, Yongping Chai, Baohui Chen, Shiya Cheng, Dong Tian, Xiaochen Wang, Ronald D. Vale, and Guangshuo Ou
http://jcb.rupress.org/cgi/content/abstract/197/1/27?etoc

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Reviews
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BH3-only proteins in apoptosis at a glance
Lina Happo, Andreas Strasser, and Suzanne Cory
http://jcs.biologists.org/cgi/content/full/125/5/1081

Non-apoptotic functions of apoptosis-regulatory proteins
Galluzzi, Kroemer and colleagues summarize the important roles of apoptotic regulators and executioners in non-lethal physiological processes as diverse as cell cycle progression, differentiation, metabolism, autophagy and inflammation.
Lorenzo Galluzzi, Oliver Kepp, Christina Trojel-Hansen and Guido Kroemer
http://www.nature.com/embor/journal/v13/n4/full/embor201219a.html

How apoptotic cells aid in the removal of their own cold dead bodies
G Wickman, L Julian and M F Olson
http://www.nature.com/cdd/journal/v19/n5/abs/cdd201225a.html

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Comments
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Mousing around with caspases and IAPs
Robert C. Rickert, Guy S. Salvesen and Carl F. Ware
http://www.biochemj.org/bj/443/bj443e001.htm

Mitochondria, Apoptosis, and the Inflammasome
Oxidized DNA released from damaged mitochondria directly activates the NLRP3 inflammasome to stimulate inflammation.
http://stke.sciencemag.org/cgi/content/abstract/sigtrans;5/219/ec106

FOXO3, ROS and apoptosis
http://jcs.biologists.org/cgi/content/full/125/5/e504

 

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