Bmf: A proapoptotic BH3-only protein regulated by interaction with the myosin V actin motor complex, activated by anoikis

Citation
H. Puthalakath et al., Bmf: A proapoptotic BH3-only protein regulated by interaction with the myosin V actin motor complex, activated by anoikis, SCIENCE, 293(5536), 2001, pp. 1829-1832
Citations number
23
Categorie Soggetti
Multidisciplinary,Multidisciplinary,Multidisciplinary
Journal title
SCIENCE
ISSN journal
00368075 → ACNP
Volume
293
Issue
5536
Year of publication
2001
Pages
1829 - 1832
Database
ISI
SICI code
0036-8075(20010907)293:5536<1829:BAPBPR>2.0.ZU;2-Q
Abstract
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 dom ain is required both for binding to prosurvival Bcl-2 proteins and for trig gering apoptosis. In healthy cells, Bmf is sequestered to myosin V motors b y association with dynein light chain 2. Certain damage signals, such as lo ss of cell attachment (anoikis), unleash Bmf, allowing it to translocate an d bind prosurvival. Bcl-2 proteins. Thus, at least two mammalian BH3-only p roteins, Bmf and Bim, function to sense intracellular damage by their local ization to distinct cytoskeletal structures.