Bcl-w(edding) with mitochondria

Trends in Cell Biology

Volumn 14, Issue 1, 2004, Pages 8-12

  Kaufmann, Thomas ^a   Schinzel, Anna ^a   Borner, Christoph ^a  

^a UNIVERSITY OF FREIBURG   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

BH3 PROTEIN; BIM PROTEIN; MUTANT PROTEIN; PROTEIN BAX; PROTEIN BCL 2; PROTEIN BCL W;

APOPTOSIS; BINDING COMPETITION; BIOSENSOR; CARBOXY TERMINAL SEQUENCE; CELL SURVIVAL; EXPERIMENTAL MODEL; HYDROPHOBICITY; MITOCHONDRIAL MEMBRANE; MITOCHONDRION; OUTER MEMBRANE; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FAMILY; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN STRUCTURE; REGULATORY MECHANISM; REVIEW; SURFACE PLASMON RESONANCE;

EID: 0346655149     PISSN: 09628924     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tcb.2003.11.005     Document Type: Short Survey

References (24)

1. Borner C. The Bcl-2 protein family: sensors and checkpoints for life-or-death decisions. Mol. Immunol. 39:2003;615-647.
2. Wilson-Annan J., et al. Proapoptotic BH3-only proteins trigger membrane integration of prosurvival Bcl-w and neutralize its activity. J. Cell Biol. 162:2003;877-887.
3. Chen-Levy Z., Cleary M.L. Membrane topology of the Bcl-2 proto-oncogenic protein demonstrated in vitro. J. Biol. Chem. 265:1990;4929-4933.
4. Lithgow T.R., et al. The protein product of the oncogene Bcl-2 is a component of the nuclear envelope, the endoplasmic reticulum, and the outer mitochondrial membrane. Cell Growth Differ. 5:1994;411-417.
5. L, but not Bcl-2, to the mitochondrial outer membrane. J. Cell Biol. 160:2003;53-64.
6. Huang D.C., Strasser A. BH3-Only proteins - essential initiators of apoptotic cell death. Cell. 103:2000;839-842.
7. Muchmore S.W., et al. X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death. Nature. 381:1996;335-341.
8. Petros A.M., et al. Solution structure of the antiapoptotic protein bcl-2. Proc. Natl. Acad. Sci. U. S. A. 98:2001;3012-3017.
9. Denisov A.Y., et al. Solution structure of human Bcl-w: modulation of ligand binding by the C-terminal helix. J. Biol. Chem. 278:2003;21124-21128.
10. Hinds M.G., et al. The structure of Bcl-w reveals a role for the C-terminal residues in modulating biological activity. EMBO J. 22:2003;1497-1507.
11. Suzuki M., et al. Structure of Bax: coregulation of dimer formation and intracellular localization. Cell. 103:2000;645-654.
12. Horie C., et al. Characterization of signal that directs C-tail-anchored proteins to mammalian mitochondrial outer membrane. Mol. Biol. Cell. 13:2002;1615-1625.
13. Antonsson B., et al. Bax is present as a high molecular weight oligomer/complex in the mitochondrial membrane of apoptotic cells. J. Biol. Chem. 276:2001;11615-11623.
14. Nechushtan A., et al. Bax and Bak coalesce into novel mitochondria-associated clusters during apoptosis. J. Cell Biol. 153:2001;1265-1276.
15. Wolter K.G., et al. Movement of Bax from the cytosol to mitochondria during apoptosis. J. Cell Biol. 139:1997;1281-1292.
16. Nechushtan A., et al. Conformation of the Bax C-terminus regulates subcellular location and cell death. EMBO J. 18:1999;2330-2341.
17. Desagher S., et al. Bid-induced conformational change of Bax is responsible for mitochondrial cytochrome c release during apoptosis. J. Cell Biol. 144:1999;891-901.
18. Guo B., et al. Humanin peptide suppresses apoptosis by interfering with Bax activation. Nature. 423:2003;456-461.
19. Nomura M., et al. 14-3-3 Interacts directly with and negatively regulates pro-apoptotic Bax. J. Biol. Chem. 278:2003;2058-2065.
20. Ruffolo S.C., et al. BID-dependent and BID-independent pathways for BAX insertion into mitochondria. Cell Death Differ. 7:2000;1101-1108.
21. Hsu Y.-T., et al. Cytosol-to-membrane redistribution of Bax and Bcl-XL during apoptosis. Proc. Natl. Acad. Sci. U. S. A. 94:1997;3668-3672.
22. Hausmann G., et al. Pro-apoptotic apoptosis protease-activating factor 1 (Apaf-1) has a cytoplasmic localization distinct from Bcl-2 or Bcl-x(L). J. Cell Biol. 149:2000;623-634.
23. Nijhawan D., et al. Elimination of Mcl-1 is required for the initiation of apoptosis following ultraviolet irradiation. Genes Dev. 17:2003;1475-1486.
24. Lackmann M., et al. Ligand for EPH-related kinase (LERK) 7 is the preferred high affinity ligand for the HEK receptor. J. Biol. Chem. 272:1997;16521-16530.