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Science 7 September 2001:
Vol. 293. no. 5536, pp. 1829 - 1832
DOI: 10.1126/science.1062257

Reports

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

Hamsa Puthalakath,1 Andreas Villunger,1 Lorraine A. O'Reilly,1 Jennifer G. Beaumont,1 Leigh Coultas,1 Richard E. Cheney,2 David C. S. Huang,1 Andreas Strasser1*

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.

1 The Walter and Eliza Hall Institute of Medical Research, Melbourne, P.O. Royal Melbourne Hospital, 3050 VIC, Australia.
2 University of North Carolina, Chapel Hill, NC 27599-7545, USA
*   To whom correspondence should be addressed. E-mail: strasser{at}wehi.edu.au


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