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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.

Pubmed ID: 10198631

Authors

  • Puthalakath H
  • Huang DC
  • O'Reilly LA
  • King SM
  • Strasser A

Journal

Molecular cell

Publication Data

March 26, 1999

Associated Grants

  • Agency: NIGMS NIH HHS, Id: GM51293

Mesh Terms

  • Amino Acid Sequence
  • Animals
  • Apoptosis
  • Apoptosis Regulatory Proteins
  • Binding Sites
  • Carrier Proteins
  • Caspase Inhibitors
  • 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