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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1999-4-26
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pubmed:abstractText |
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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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Apoptosis Regulatory Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Bcl-2-like protein 11,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Caspases,
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Dyneins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Molecular Motor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Isoforms,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-bcl-2
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
1097-2765
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
3
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
287-96
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pubmed:dateRevised |
2009-12-11
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pubmed:meshHeading |
pubmed-meshheading:10198631-Amino Acid Sequence,
pubmed-meshheading:10198631-Animals,
pubmed-meshheading:10198631-Apoptosis,
pubmed-meshheading:10198631-Apoptosis Regulatory Proteins,
pubmed-meshheading:10198631-Binding Sites,
pubmed-meshheading:10198631-Carrier Proteins,
pubmed-meshheading:10198631-Caspases,
pubmed-meshheading:10198631-Cell Line,
pubmed-meshheading:10198631-Dimerization,
pubmed-meshheading:10198631-Drosophila Proteins,
pubmed-meshheading:10198631-Dyneins,
pubmed-meshheading:10198631-Gene Library,
pubmed-meshheading:10198631-Humans,
pubmed-meshheading:10198631-Membrane Proteins,
pubmed-meshheading:10198631-Mice,
pubmed-meshheading:10198631-Microtubules,
pubmed-meshheading:10198631-Molecular Motor Proteins,
pubmed-meshheading:10198631-Molecular Sequence Data,
pubmed-meshheading:10198631-Mutation,
pubmed-meshheading:10198631-Precipitin Tests,
pubmed-meshheading:10198631-Protein Binding,
pubmed-meshheading:10198631-Protein Isoforms,
pubmed-meshheading:10198631-Proto-Oncogene Proteins,
pubmed-meshheading:10198631-Proto-Oncogene Proteins c-bcl-2,
pubmed-meshheading:10198631-Saccharomyces cerevisiae
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pubmed:year |
1999
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pubmed:articleTitle |
The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex.
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pubmed:affiliation |
Walter and Eliza Hall Institute of Medical Research, Royal Melbourne Hospital, Victoria, Australia.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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