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

Author(s): Puthalakath, H; Villunger, A; O'Reilly, LA; Beaumont, JG; Coultas, L; Cheney, RE; Huang, DCS; Strasser, A;
Details: Publication Year 2001-09-07,Volume 293,Issue #5536,Page 1829-1832
Journal Title: SCIENCE
Publication Type: Journal Article
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 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.
Publisher: AMER ASSOC ADVANCEMENT SCIENCE
Keywords: BCL-2 FAMILY; LIGHT-CHAIN; CELL-DEATH; APOPTOSIS; DYNEIN; MEMBER; BIM; PURIFICATION; INTEGRINS
Publisher's Version: https://doi.org/10.1126/science.1062257
Terms of Use/Rights Notice: Refer to copyright notice on published article.

Creation Date: 2001-09-07 12:00:00