4.8 Article

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

Journal

SCIENCE
Volume 293, Issue 5536, Pages 1829-1832

Publisher

AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1062257

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Funding

  1. NCI NIH HHS [CA 80188] Funding Source: Medline
  2. NIDCD NIH HHS [R29 DC003299] Funding Source: Medline

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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.

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