The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex |
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Authors: | Puthalakath H Huang D C O'Reilly L A King S M Strasser A |
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Institution: | Walter and Eliza Hall Institute of Medical Research, Royal Melbourne Hospital, Victoria, Australia. |
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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 Bim. In healthy cells, most Bim 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 Bim 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. |
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