Bmf: A Proapoptotic BH3-Only Protein Regulated by Interaction with the Myosin V Actin Motor Complex, Activated by Anoikis

Bcl-2 family members bearing only the BH3 domain are essential inducers of apoptosis. We identified a BH3-only protein, Bmf, and show that its BH3 domain is required both for binding to prosurvival Bcl-2 proteins and for triggering apoptosis. In healthy cells, Bmf is sequestered to myosin V motors b...

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Veröffentlicht in:Science (American Association for the Advancement of Science) 2001-09, Vol.293 (5536), p.1829-1832
Hauptverfasser: Puthalakath, Hamsa, Villunger, Andreas, O'Reilly, Lorraine A., Beaumont, Jennifer G., Coultas, Leigh, Cheney, Richard E., David C. S. Huang, Strasser, Andreas
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Sprache:eng
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Zusammenfassung:Bcl-2 family members bearing only the BH3 domain are essential inducers of apoptosis. We identified a BH3-only protein, Bmf, and show that its BH3 domain is required both for binding to prosurvival Bcl-2 proteins and for triggering apoptosis. In healthy cells, Bmf is sequestered to myosin V motors by association with dynein light chain 2. Certain damage signals, such as loss of cell attachment (anoikis), unleash Bmf, allowing it to translocate and bind prosurvival Bcl-2 proteins. Thus, at least two mammalian BH3-only proteins, Bmf and Bim, function to sense intracellular damage by their localization to distinct cytoskeletal structures.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.1062257