ApoList – November 2021


Caspases and IAPs


Caspase-2 regulates S-phase cell cycle events to protect from DNA damage accumulation independent of apoptosis – Ashley G. Boice, Karla E. Lopez, Raj K. Pandita, Melissa J. Parsons, Chloe I. Charendoff, Vijay Charaka, Alexandre F. Carisey, Tej K. Pandita and Lisa Bouchier-Hayes. https://www.nature.com/articles/s41388-021-02085-w
XIAP restrains TNF-driven intestinal inflammation and dysbiosis by promoting innate immune responses of Paneth and dendritic cells – Adam Wahida, Madeleine Müller, Andreas Hiergeist, Bastian Popper, Katja Steiger, Caterina Branca, Markus Tschurtschenthaler, Thomas Engleitner, Sainitin Donakonda, Jordy De Coninck, Rupert Öllinger, Marie K. Pfautsch, Nicole Müller, Miguel Silva, Sinem Usluer, Erik Thiele Oberg, Jan P. Böttcher, Nicole Pfarr, Martina Anton, Julia B. Slotta-Huspenina, Andreas G. Nerlich, Tobias Madl, Marijana Basic, André Bleich, Geert Berx, Jürgen Ruland, Percy A. Knolle, Roland Rad, Timon E. Adolph, Peter Vandenabeele, Hirokazu Kanegane, André Gessner, Philipp J. Jost, Monica Yabal. https://www.science.org/doi/full/10.1126/sciimmunol.abf7235
Deficiency in X-linked inhibitor of apoptosis protein promotes susceptibility to microbial triggers of intestinal inflammation – Anne Strigli, Shreya Gopalakrishnan, Yvonne Zeissig, Marijana Basic, Jun Wang, Tobias Schwerd, Shauni Doms, Kenneth Peuker, Jelka Hartwig, Jürgen Harder, Pia Hönscheid, Philipp Arnold, Thomas Kurth, Fabian Rost, Britt-Sabina Petersen, Michael Forster, Andre Franke, Judith R. Kelsen, Meino Rohlfs, Christoph Klein, Aleixo M. Muise, Neil Warner, Ryusuke Nambu, Julia Mayerle, Helga-Paula Török, Andreas Linkermann, Michael H. Muders, Gustavo B. Baretton, Jochen Hampe, Daniela E. Aust, John F. Baines, André Bleich, Sebastian Zeissig. https://www.science.org/doi/full/10.1126/sciimmunol.abf7473
SMAC/Diablo controls proliferation of cancer cells by regulating phosphatidylethanolamine synthesis – Swaroop Kumar Pandey, Avijit Paul, Anna Shteinfer-Kuzmine, Ran Zalk, Uwe Bunz, Varda Shoshan-Barmatz. https://febs.onlinelibrary.wiley.com/doi/full/10.1002/1878-0261.12959


Efferocytosis, entosis, cell-cell


Apoptotic stress-induced FGF signalling promotes non-cell autonomous resistance to cell death – Florian J. Bock, Egor Sedov, Elle Koren, Anna L. Koessinger, Catherine Cloix, Désirée Zerbst, Dimitris Athineos, Jayanthi Anand, Kirsteen J. Campbell, Karen Blyth, Yaron Fuchs and Stephen W. G. Tait. https://www.nature.com/articles/s41467-021-26613-0
TRAIL signaling promotes entosis in colorectal cancer – Emir Bozkurt; Heiko Düssmann; Manuela Salvucci; Brenton L. Cavanagh ; Sandra Van Schaeybroeck; Daniel B. Longley; Seamus J. Martin; Jochen H.M. Prehn. https://rupress.org/jcb/article-abstract/220/11/e202010030/212649
Human intestinal and circulating invariant natural killer T cells are cytotoxic against colorectal cancer cells via the perforin–granzyme pathway – Angélica Díaz-Basabe, Claudia Burrello, Georgia Lattanzi, Fiorenzo Botti, Alberto Carrara, Elisa Cassinotti, Flavio Caprioli, Federica Facciotti. https://febs.onlinelibrary.wiley.com/doi/full/10.1002/1878-0261.13104


Death receptors


HOIP limits anti‐tumor immunity by protecting against combined TNF and IFN‐gamma‐induced apoptosis – Andrew J Freeman, Stephin J Vervoort, Jessica Michie, Kelly M Ramsbottom, John Silke, Conor J Kearney, Jane Oliaro. https://www.embopress.org/doi/abs/10.15252/embr.202153391
A patch of positively charged residues regulates the efficacy of clinical DR5 antibodies in solid tumors – Gururaj Shivange, Tanmoy Mondal, Evan Lyerly, Sanchita Bhatnagar, Charles N. Landen, Shivani Reddy, Jonathan Kim, Britney Doan, Paula Riddle, Jogender Tushir-Singh. https://www.cell.com/cell-reports/fulltext/S2211-1247(21)01430-3
A comprehensive interaction study provides a potential domain interaction network of human death domain superfamily proteins – Wei Zhou, Naoe Kaneko, Tomoya Nakagita, Hiroyuki Takeda and Junya Masumoto. https://www.nature.com/articles/s41418-021-00796-x
TRAIL/DR5 pathway promotes AKT phosphorylation, skeletal muscle differentiation, and glucose uptake – Barbara Toffoli, Federica Tonon, Veronica Tisato, Giorgio Zauli, Paola Secchiero, Bruno Fabris and Stella Bernardi. https://www.nature.com/articles/s41419-021-04383-3


Necroptosis, RIP kinases, MLKL


Oligomerization‐driven MLKL ubiquitylation antagonizes necroptosis – Zikou Liu, Laura F Dagley, Kristy Shield-Artin, Samuel N Young, Aleksandra Bankovacki, Xiangyi Wang, Michelle Tang, Jason Howitt, Che A Stafford, Ueli Nachbur, Cheree Fitzgibbon, Sarah E Garnish, Andrew I Webb, David Komander, James M Murphy, Joanne M Hildebrand, John Silke. https://www.embopress.org/doi/abs/10.15252/embj.2019103718
Human RIPK3 maintains MLKL in an inactive conformation prior to cell death by necroptosis – Yanxiang Meng, Katherine A. Davies and James M. Murphy. https://www.nature.com/articles/s41467-021-27032-x
MLKL promotes cellular differentiation in myeloid leukemia by facilitating the release of G-CSF – Xin Wang, Uris Ros, Deepti Agrawal, Eva C. Keller, Julia Slotta-Huspenina, Veronika Dill, Bo Shen, Run Shi, Tobias Herold, Claus Belka, Ritu Mishra, Florian Bassermann, Ana J. Garcia-Saez and Philipp J. Jost. https://www.nature.com/articles/s41418-021-00811-1
Caspase‐9 acts as a regulator of necroptotic cell death – Tamás Molnár, Petra Pallagi, Bálint Tél, Róbert Király, Eszter Csoma, Viktória Jenei, Zsófia Varga, Péter Gogolák, Anne Odile Hueber, Zoltán Máté, Ferenc Erdélyi, Gábor Szabó, Aladár Pettkó-Szandtner, Attila Bácsi, László Virág, József Maléth, Gábor Koncz. https://febs.onlinelibrary.wiley.com/doi/full/10.1111/febs.15898
Quantitative analysis of phosphoproteome in necroptosis reveals a role of TRIM28 phosphorylation in promoting necroptosis-induced cytokine production – Rui Zu, Zhen Yu, Jing Zhao, Xiaojuan Lu, Wei Liang, Le Sun, Chenfang Si, Kezhou Zhu, Tian Zhang, Ganquan Li, Mengmeng Zhang, Yaoyang Zhang, Nan Liu, Junying Yuan and Bing Shan. https://www.nature.com/articles/s41419-021-04290-7
Genetic inhibition of RIPK3 ameliorates functional outcome in controlled cortical impact independent of necroptosis – Limin Wu, Joon Yong Chung, Tian Cao, Gina Jin, William J. Edmiston III, Suzanne Hickman, Emily S. Levy, Jordyn A. Whalen, Eliza Sophie LaRovere Abrams, Alexei Degterev, Eng H. Lo, Lorenzo Tozzi, David L. Kaplan, Joseph El Khoury and Michael J. Whalen. https://www.nature.com/articles/s41419-021-04333-z
Proteomic analysis of necroptotic extracellular vesicles – Inbar Shlomovitz, Ziv Erlich, Gali Arad, Liat Edry-Botzer, Sefi Zargarian, Hadar Cohen, Tal Manko, Yifat Ofir-Birin, Tomer Cooks, Neta Regev-Rudzki and Motti Gerlic. https://www.nature.com/articles/s41419-021-04317-z


Reviews


Molecular mechanisms and functions of pyroptosis in inflammation and antitumor immunity – Junwei Hou, Jung-Mao Hsu, Mien-Chie Hung. https://www.cell.com/molecular-cell/fulltext/S1097-2765(21)00737-1
Soluble CD95L in cancers and chronic inflammatory disorders, a new therapeutic target? – Keerthi Kurma, Andrea Boizard-Moracchini, Gael Galli, Mickael Jean, Pierre Vacher, Patrick Blanco, Patrick Legembre. https://www.sciencedirect.com/science/article/abs/pii/S0304419X21000937
First we eat, then we do everything else: The dynamic metabolic regulation of efferocytosis – Alissa Trzeciak, Ya-Ting Wang, Justin Shaun Arnold Perry. https://www.cell.com/cell-metabolism/fulltext/S1550-4131(21)00364-8
Apoptotic cell-derived metabolites in efferocytosis-mediated resolution of inflammation – Yiwei Mao. https://www.sciencedirect.com/science/article/abs/pii/S1359610121000745
Dying cells fan the flames of inflammation – Kim Newton, Vishva M. Dixit, Nobuhiko Kayagaki. https://www.science.org/doi/10.1126/science.abi5934#.YaAPliOd4NI


Comments


Cell death leaves a new TRAIL – Michael Overholtzer. https://rupress.org/jcb/article/220/11/e202109018/212699
In Conversation with Tony Letai – Eleni Skourti, Anthony Letai. https://febs.onlinelibrary.wiley.com/doi/full/10.1111/febs.16229
Editor Profile: Eli Arama. https://febs.onlinelibrary.wiley.com/doi/full/10.1111/febs.15902
Bcl-xL and IP3R interaction: Intimate relationship with an uncertain outcome – Nikolay Popgeorgieva, Germain Gillet. https://www.sciencedirect.com/science/article/abs/pii/S0143416021001585


Bcl-2 family proteins


Bcl-xL acts as an inhibitor of IP3R channels, thereby antagonizing Ca2+-driven apoptosis – Nicolas Rosa, Hristina Ivanova, Larry E. Wagner 2nd, Justin Kale, Rita La Rovere, Kirsten Welkenhuyzen, Nikolaos Louros, Spyridoula Karamanou, Victoria Shabardina, Irma Lemmens, Elien Vandermarliere, Kozo Hamada, Hideaki Ando, Frederic Rousseau, Joost Schymkowitz, Jan Tavernier, Katsuhiko Mikoshiba, Anastassios Economou, David W. Andrews, Jan B. Parys, David I. Yule and Geert Bultynck. https://www.nature.com/articles/s41418-021-00894-w
BH3-only proteins Puma and Beclin1 regulate autophagic death in neurons in response to Amyloid-β – Akash Saha, Suraiya Saleem, Paidi Ramesh Kumar and Subhas C. Biswas. https://www.nature.com/articles/s41420-021-00748-x
The BAX-binding protein MOAP1 associates with LC3 and promotes closure of the phagophore – Hao-Chun Chang, Ran N. Tao, Chong Teik Tan, Ya Jun Wu, Boon Huat Bay and Victor C. Yu. https://www.tandfonline.com/doi/full/10.1080/15548627.2021.1896157
Venetoclax imparts distinct cell death sensitivity and adaptivity patterns in T cells – Lindsey M. Ludwig, Katrina M. Hawley, David B. Banks, Anika T. Thomas-Toth, Bruce R. Blazar, Megan E. McNerney, Joel D. Leverson and James L. LaBelle. https://www.nature.com/articles/s41419-021-04285-4
Development of a BCL-xL and BCL-2 dual degrader with improved anti-leukemic activity – Dongwen Lv, Pratik Pal, Xingui Liu, Yannan Jia, Dinesh Thummuri, Peiyi Zhang, Wanyi Hu, Jing Pei, Qi Zhang, Shuo Zhou, Sajid Khan, Xuan Zhang, Nan Hua, Qingping Yang, Sebastian Arango, Weizhou Zhang, Digant Nayak, Shaun K. Olsen, Susan T. Weintraub, Robert Hromas, Marina Konopleva, Yaxia Yuan, Guangrong Zheng and Daohong Zhou. https://www.nature.com/articles/s41467-021-27210-x
Paradoxical implication of BAX/BAK in the persistence of tetraploid cells – Jiayin Deng, Lucía G. Gutiérrez, Gautier Stoll, Omar Motiño, Isabelle Martins, Lucía Núñez, José Manuel Bravo-San Pedro, Juliette Humeau, Chloé Bordenave, Juncheng Pan, Hélène Fohrer-Ting, Sylvie Souquere, Gerard Pierron, Claudio Hetz, Carlos Villalobos, Guido Kroemer and Laura Senovilla. https://www.nature.com/articles/s41419-021-04321-3
UBQLN4 is an ATM substrate that stabilizes the anti‐apoptotic proteins BCL2A1 and BCL2L10 in mesothelioma – Fang Liu, RunSang Pan, HongYu Ding, LiLing Gu, Yun Yang, ChuanYin Li, YongJie Xu, Ronggui Hu, Hui Chen, XiangYan Zhang, YingJie Nie. https://febs.onlinelibrary.wiley.com/doi/full/10.1002/1878-0261.13058
BAX mitochondrial integration is regulated allosterically by its α1−α2 loop – Michael A. Dengler, Leonie Gibson and Jerry M. Adams. https://www.nature.com/articles/s41418-021-00815-x


Pyroptosis


Gasdermin D mediates host cell death bu not interleukin-1β secretion in Mycobacterium tuberculosis-infected macrophages – Sebastian J. Theobald, Jessica Gräb, Melanie Fritsch, Isabelle Suárez, Hannah S. Eisfeld, Sandra Winter, Maximilian Koch, Christoph Hölscher, Manolis Pasparakis, Hamid Kashkar and Jan Rybniker. https://www.nature.com/articles/s41420-021-00716-5

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

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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

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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

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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

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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