Regulating cell death at, on, and in membranes

被引:57
作者
Chi, Xiaoke [1 ]
Kale, Justin [2 ]
Leber, Brian [3 ]
Andrews, David W. [1 ,2 ,4 ,5 ]
机构
[1] McMaster Univ, Dept Chem & Chem Biol, Hamilton, ON L8N 3Z5, Canada
[2] McMaster Univ, Dept Biochem & Biomed Sci, Hamilton, ON L8N 3Z5, Canada
[3] McMaster Univ, Dept Med, Hamilton, ON L8N 3Z5, Canada
[4] Sunnybrook Res Inst, Toronto, ON M4N 3M5, Canada
[5] Univ Toronto, Dept Biochem, Toronto, ON, Canada
来源
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH | 2014年 / 1843卷 / 09期
基金
加拿大健康研究院;
关键词
Apoptosis; Bcl-2; family; Endoplasmic reticulum; Mitochondrion; Membrane; Embedded Together; ENDOPLASMIC-RETICULUM STRESS; BCL-2; FAMILY-MEMBER; MITOCHONDRIAL OUTER-MEMBRANE; CYTOCHROME-C RELEASE; BH3-ONLY PROTEIN BIM; ANTI-APOPTOTIC MCL-1; ER STRESS; CONFORMATIONAL-CHANGES; BAX ACTIVATION; PEPTIDE COMPLEX;
D O I
10.1016/j.bbamcr.2014.06.002
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Bcl-2 family proteins are central regulators of apoptosis. Various family members are located in the cytoplasm, endoplasmic reticulum, and mitochondrial outer membrane in healthy cells. However during apoptosis most of the interactions between family members that determine the fate of the cell occur at the membranes of intracellular organelles. It has become evident that interactions with membranes play an active role in the regulation of Bcl-2 family protein interactions. Here we provide an overview of various models proposed to explain how the Bcl-2 family regulates apoptosis and discuss how membrane binding affects the structure and function of each of the three categories of Bcl-2 proteins (pro-apoptotic, pore-forming, and anti-apoptotic). We also examine how the Bcl-2 family regulates other aspects of mitochondrial and ER physiology relevant to cell death. (C) 2014 Published by Elsevier B.V.
引用
收藏
页码:2100 / 2113
页数:14
相关论文
共 230 条
[1]   Navitoclax (ABT-263) and bendamustine ± rituximab induce enhanced killing of non-Hodgkin's lymphoma tumours in vivo [J].
Ackler, S. ;
Mitten, M. J. ;
Chen, J. ;
Clarin, J. ;
Foster, K. ;
Jin, S. ;
Phillips, D. C. ;
Schlessinger, S. ;
Wang, B. ;
Leverson, J. D. ;
Boghaert, E. R. .
BRITISH JOURNAL OF PHARMACOLOGY, 2012, 167 (04) :881-891
[2]   Organization of the Mitochondrial Apoptotic BAK Pore OLIGOMERIZATION OF THE BAK HOMODIMERS [J].
Aluvila, Sreevidya ;
Mandal, Tirtha ;
Hustedt, Eric ;
Fajer, Peter ;
Choe, Jun Yong ;
Oh, Kyoung Joon .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2014, 289 (05) :2537-2551
[3]   Rax forms multispanning monomers that oligomerize to permeabilize membranes during apoptosis [J].
Annis, MG ;
Dlugosz, PJ ;
Cruz-Aguado, JA ;
Penn, LZ ;
Leber, B ;
Andrews, DW .
EMBO JOURNAL, 2005, 24 (12) :2096-2103
[4]   Endoplasmic reticulum localized Bcl-2 prevents apoptosis when redistribution of cytochrome c is a late event [J].
Annis, MG ;
Zamzami, N ;
Zhu, WJ ;
Penn, LZ ;
Kroemer, G ;
Leber, B ;
Andrews, DW .
ONCOGENE, 2001, 20 (16) :1939-1952
[5]   Differences in the Mechanisms of Proapoptotic BH3 Proteins Binding to Bcl-XL and Bcl-2 Quantified in Live MCF-7 Cells [J].
Aranovich, Alexander ;
Liu, Qian ;
Collins, Tony ;
Geng, Fei ;
Dixit, Sudeepa ;
Leber, Brian ;
Andrews, David W. .
MOLECULAR CELL, 2012, 45 (06) :754-763
[6]   Bax-type apoptotic proteins porate pure lipid bilayers through a mechanism sensitive to intrinsic monolayer curvature [J].
Basañez, G ;
Sharpe, JC ;
Galanis, J ;
Brandt, TB ;
Hardwick, JM ;
Zimmerberg, J .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (51) :49360-49365
[7]   Bax, but not Bcl-xL, decreases the lifetime of planar phospholipid bilayer membranes at subnanomolar concentrations [J].
Basañez, G ;
Nechushtan, A ;
Drozhinin, O ;
Chanturiya, A ;
Choe, E ;
Tutt, S ;
Wood, KA ;
Hsu, YT ;
Zimmerberg, J ;
Youle, RJ .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1999, 96 (10) :5492-5497
[8]   Bcl-xL increases mitochondrial fission, fusion, and biomass in neurons [J].
Berman, Sarah B. ;
Chen, Ying-bei ;
Qi, Bing ;
McCaffery, J. Michael ;
Rucker, Edmund B., III ;
Goebbels, Sandra ;
Nave, Klaus-Armin ;
Arnold, Beth A. ;
Jonas, Elizabeth A. ;
Pineda, Fernando J. ;
Hardwick, J. Marie .
JOURNAL OF CELL BIOLOGY, 2009, 184 (05) :707-719
[9]   The landscape of somatic copy-number alteration across human cancers [J].
Beroukhim, Rameen ;
Mermel, Craig H. ;
Porter, Dale ;
Wei, Guo ;
Raychaudhuri, Soumya ;
Donovan, Jerry ;
Barretina, Jordi ;
Boehm, Jesse S. ;
Dobson, Jennifer ;
Urashima, Mitsuyoshi ;
Mc Henry, Kevin T. ;
Pinchback, Reid M. ;
Ligon, Azra H. ;
Cho, Yoon-Jae ;
Haery, Leila ;
Greulich, Heidi ;
Reich, Michael ;
Winckler, Wendy ;
Lawrence, Michael S. ;
Weir, Barbara A. ;
Tanaka, Kumiko E. ;
Chiang, Derek Y. ;
Bass, Adam J. ;
Loo, Alice ;
Hoffman, Carter ;
Prensner, John ;
Liefeld, Ted ;
Gao, Qing ;
Yecies, Derek ;
Signoretti, Sabina ;
Maher, Elizabeth ;
Kaye, Frederic J. ;
Sasaki, Hidefumi ;
Tepper, Joel E. ;
Fletcher, Jonathan A. ;
Tabernero, Josep ;
Baselga, Jose ;
Tsao, Ming-Sound ;
Demichelis, Francesca ;
Rubin, Mark A. ;
Janne, Pasi A. ;
Daly, Mark J. ;
Nucera, Carmelo ;
Levine, Ross L. ;
Ebert, Benjamin L. ;
Gabriel, Stacey ;
Rustgi, Anil K. ;
Antonescu, Cristina R. ;
Ladanyi, Marc ;
Letai, Anthony .
NATURE, 2010, 463 (7283) :899-905
[10]   The endoplasmic reticulum: a multifunctional signaling organelle [J].
Berridge, MJ .
CELL CALCIUM, 2002, 32 (5-6) :235-249