Bax and Bif-1 proteins interact on Bilayer Lipid Membrane and form pore

Biochemical and Biophysical Research Communications

Volumn 463, Issue 4, 2015, Pages 751-755

  Gupta, Rajeev ^a   Ghosh, Subhendu ^a  

^a UNIVERSITY OF DELHI   (India)

Author keywords

Bax; Bif 1; Bilayer electrophysiology; Mitochondria mediated apoptosis; Pore

Indexed keywords

BAX INTERACTING FACTOR 1 PROTEIN; CELL PROTEIN; ION CHANNEL; PROTEIN BAX; UNCLASSIFIED DRUG; LIPID BILAYER; PROTEIN BINDING; SH3GLB1 PROTEIN, HUMAN; SIGNAL TRANSDUCING ADAPTOR PROTEIN;

APOPTOSIS; ARTICLE; CHANNEL GATING; CONDUCTANCE; CONFORMATIONAL TRANSITION; ELECTRIC POTENTIAL; ELECTROPHYSIOLOGY; LIPID BILAYER; MITOCHONDRION; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; PROTEIN TRANSPORT; METABOLISM; PATCH CLAMP TECHNIQUE;

ADAPTOR PROTEINS, SIGNAL TRANSDUCING; BCL-2-ASSOCIATED X PROTEIN; LIPID BILAYERS; PATCH-CLAMP TECHNIQUES; PROTEIN BINDING;

EID: 84936986428     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2015.06.007     Document Type: Article

References (26)

1. L. Lalier, P.F. Cartron, P. Juin, S. Nedelkina, S. Manon, B. Bechinger, and F.M. Vallette Bax activation and mitochondrial insertion during apoptosis Apoptosis 12 5 2007 887 896 10.1007/s10495.007.0749.1
2. A. Gross, J. Jockel, M.C. Wei, and S.J. Korsmeyer Enforced dimerization of bax results in its translocation, mitochondrial dysfunction and apoptosis EMBO J. 17 14 1998 3878 3885 10.1093/emboj/17.14.3878
3. S.H. Lin, M.N. Perera, T. Nguyen, D. Datskovskiy, M. Miles, and M. Colombini Bax forms two types of channels, one of which is voltage-gated Biophys. J. 101 2011 2163 2169 10.1016/j.bpj.2011.09.041
4. J. Banerjee, and S. Ghosh Bax increases the pore size of rat brain mitochondrial voltage-dependent anion channel in the presence of tBid Biochim. Biophys. Res. Commun. 323 1 2004 310 314 10.1016/j.bbrc.2004.08.094
5. R.F. Epand, J.C. Martinou, S. Montessuit, and R.M. Epand Transbilayer lipid diffusion promoted by Bax: implications for apoptosis Biochemistry 42 2003 14576 14582 10.1021/bi035348w
6. O. Terrones, B. Antonsson, H. Yamaguchi, H.G. Wang, J. Liu, R.M. Lee, A. Herrmann, and G. Basañez Lipidic pore formation by the concerted action of proapoptotic BAX and tBID J. Biol. Chem. 279 29 2004 30081 30091 10.1074/jbc.M313420200
7. G. Basañez, J.C. Sharpe, J. Galanis, T.B. Brandt, J.M. Hardwick, and J. Zimmerberg Bax-type apoptotic proteins porate pure lipid bilayers through a mechanism sensitive to intrinsic monolayer curvature J. Biol. Chem. 277 51 2002 49360 49365 10.1074/jbc.M206069200
8. S. Shimizu, T. Ide, T. Yanagida, and Y. Tsujimoto Electrophysiological study of a novel large pore formed by bax and the voltage-dependent anion channel that is permeable to cytochrome c J. Biol. Chem. 275 16 2000 12321 12325 10.1074/jbc.275.16.12321
9. X. Roucou, S. Montessuit, B. Antonsson, and J.C. Martinou Bax oligomerization in mitochondrial membranes requires tBid (caspase-8-cleaved Bid) and a mitochondrial protein Biochem. J. 368 2002 915 921 10.1042/BJ20020972
10. R. Eskes, S. Desagher, B. Antonsson, and J.C. Martinou Bid induces the oligomerization and insertion of bax into the outer mitochondrial membrane Mol. Cell Biol. 20 3 2000 929 935 10.1128/MCB.20.3.929-935.2000
11. T. Gallenne, F. Gautier, L. Oliver, E. Hervouet, B. Noël, J.A. Hickman, O. Geneste, P.-F. Cartron, F.M. Vallette, S. Manon, and P. Juin Bax activation by the BH3-only protein Puma promotes cell dependence on antiapoptotic Bcl-2 family members J. Cell Biol. 185 2 2009 279 290 10.1083/jcb.200809153
12. O. Kjaerulff, L. Brodin, and A. Jung The structure and function of endophilin proteins Cell Biochem. Biophys. 60 3 2010 137 154 10.1007/s12013.010.9137-5
13. S.M. Cuddeback, H. Yamaguchi, K. Komatsu, T. Miyashita, M. Yamada, C. Wu, S. Singh, and H.G. Wang Molecular cloning and characterization of Bif-1. A novel Src homology 3 domain-containing protein that associates with bax J. Biol. Chem. 276 23 2001 20559 20565 10.1074/jbc.M101527200
14. M. Karbowski, S.Y. Jeong, and R.J. Youle Endophilin B1 is required for the maintenance of mitochondrial morphology J. Cell Biol. 166 7 2004 1027 1039 10.1083/jcb.200407046
15. S. Suresh, and J.M. Edwardson The endophilin N-BAR domain perturbs the structure of lipid bilayers Biochemistry 49 2010 5766 5771 10.1021/bi100760e
16. K. Farsad, N. Ringstad, K. Takei, S.R. Floyd, K. Rose, and P. De Camilli Generation of high curvature membranes mediated by direct endophilin bilayer interactions J. Cell Biol. 155 2 2001 193 200 10.1083/jcb.200107075
17. J.L. Gallop, C.C. Jao, H.M. Kent, P.J.G. Butler, P.R. Evans, R. Langen, and H.T. McMahon Mechanism of endophilin N-BAR domain-mediated membrane curvature EMBO J. 25 12 2006 2898 2910 10.1038/sj.emboj.7601174
18. Y. Takahashi, M. Karbowski, H. Yamaguchi, A. Kazi, J. Wu, S.M. Sebti, R.J. Youle, and H.G. Wang Loss of Bif-1 suppresses Bax/Bak conformational change and mitochondrial apoptosis Mol. Cell Biol. 25 2005 9369 9382 10.1128/MCB.25.21.9369-9382.2005
19. A. Etxebarria, O. Terrones, H. Yamaguchi, A. Landajuela, O. Landeta, B. Antonsson, H.G. Wang, and G. Basañez Endophilin B1/Bif-1 stimulates bax activation independently from its capacity to produce large-scale membrane morphological rearrangements J. Biol. Chem. 284 7 2009 4200 4212 10.1074/jbc.M808050200
20. T.K. Rostovtseva, H. Boukari, A. Antignani, B. Shiu, S. Banerjee, A. Neutzner, and R.J. Youle Bax activates Endophilin B1 oligomerization and lipid membrane vesiculation J. Biol. Chem. 284 49 2009 34390 34399 10.1074/jbc.M109.021873
21. A.K. Bera, and S. Ghosh Dual mode of gating of voltage-dependent anion channel as revealed by phosphorylation J. Struct. Biol. 135 2001 67 72 10.1006/jsbi.2001.4399
22. R. Gupta, and S. Ghosh Phosphorylation of voltage-dependent anion channel by c-Jun N-terminal Kinase-3 leads to closure of the channel Biochim. Biophys. Res. Commun. 459 1 2015 100 106 10.1016/j.bbrc.2015.02.077
23. X. Roucou, and J.C. Martinou Conformational change of Bax: a question of life or death Cell Death Differ. 18 2001 875 877 10.1038/sj.cdd.4400910
24. E. Gavathiotis, M. Suzuki, M.L. Davis, K. Pitter, G.H. Bird, S.G. Katz, H.C. Tu, H. Kim, E.H.-Y. Cheng, N. Tjandra, and L.D. Walensky Bax activation is initiated at a novel interaction site Nature 455 2008 1076 1081 10.1038/nature07396
25. J.A. Yethon, R.F. Epand, B. Leber, R.M. Epand, and D.W. Andrews Interaction with a membrane surface triggers a reversible conformational change in bax normally associated with induction of apoptosis J. Biol. Chem. 278 49 2003 48935 48941 10.1074/jbc.M306289200
26. L.M. Dejean, S. Martinez-Caballero, L. Guo, C. Hughes, O. Teijido, T. Ducret, F. Ichas, S.J. Korsmeyer, B. Antonsson, E.A. Jonas, and K.W. Kinnally Oligomeric Bax is a component of the putative cytochrome c release channel MAC, mitochondrial apoptosis-induced channel Mol. Biol. Cell 16 5 2005 2424 2432 10.1091/mbc.E04-12-1111