The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex
- Author(s)
- Puthalakath, H; Huang, DCS; O'Reilly, LA; King, SM; Strasser, A;
- Details
- Publication Year 1999-03,Volume 3,Issue #3,Page 287-296
- Journal Title
- MOLECULAR CELL
- Publication Type
- Journal Article
- Abstract
- Bcl-2 family members that have only a single Bcl-2 homology domain, BH3, are potent inducers of apoptosis, and some appear to play a critical role in developmentally programmed cell death. We examined the regulation of the proapoptotic activity of the BH3-only protein Rim. In healthy cells, most Rim molecules were bound to LC8 cytoplasmic dynein light chain and thereby sequestered to the microtubule-associated dynein motor complex. Certain apoptotic stimuli disrupted the interaction between LC8 and the dynein motor complex. This freed Rim to translocate together with LC8 to Bcl-2 and to neutralize its antiapoptotic activity. This process did not require caspase activity and therefore constitutes an initiating event in apoptosis signaling.
- Publisher
- CELL PRESS
- Keywords
- CELL-DEATH; CAENORHABDITIS-ELEGANS; LIGHT-CHAIN; PROTEIN; APOPTOSIS; CED-4; PHOSPHORYLATION; BAD; EXPRESSION; CASPASE-3
- Publisher's Version
- https://doi.org/10.1016/S1097-2765(00)80456-6
- Terms of Use/Rights Notice
- Refer to copyright notice on published article.
Creation Date: 1999-03-01 12:00:00