The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex.
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.
Mesh Terms:
Amino Acid Sequence, Animals, Apoptosis, Apoptosis Regulatory Proteins, Binding Sites, Carrier Proteins, Caspases, Cell Line, Dimerization, Drosophila Proteins, Dyneins, Gene Library, Humans, Membrane Proteins, Mice, Microtubules, Molecular Motor Proteins, Molecular Sequence Data, Mutation, Precipitin Tests, Protein Binding, Protein Isoforms, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-bcl-2, Saccharomyces cerevisiae
Amino Acid Sequence, Animals, Apoptosis, Apoptosis Regulatory Proteins, Binding Sites, Carrier Proteins, Caspases, Cell Line, Dimerization, Drosophila Proteins, Dyneins, Gene Library, Humans, Membrane Proteins, Mice, Microtubules, Molecular Motor Proteins, Molecular Sequence Data, Mutation, Precipitin Tests, Protein Binding, Protein Isoforms, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-bcl-2, Saccharomyces cerevisiae
Mol. Cell
Date: Mar. 01, 1999
PubMed ID: 10198631
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