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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
10
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pubmed:dateCreated |
2004-5-19
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pubmed:abstractText |
Bcl-x(L) is a potent inhibitor of apoptosis. While Bcl-x(L) can be bound to mitochondria, a substantial fraction, depending on the cell type or tissue, is found in the cytosol of healthy cells. Gel filtration and crosslinking experiments reveal that, unlike monomeric Bax, Bcl-x(L) migrates in a complex of approximately 50 kDa in the cytosol. Co-immunoprecipitation experiments indicate that Bcl-x(L) in the cytosol forms homodimers. The C-terminal hydrophobic tails of two Bcl-x(L) molecules are involved in homodimer formation, and analysis of mutants demonstrates that the C-terminal lysine residue and the G138 residue lining the BH3-binding pocket are required for homodimerization. The flexible loop preceding the C-terminal tail in Bcl-x(L) is longer than that of several monomeric Bcl-2 family members and is a requisite for the homodimer formation. Bad binding to Bcl-x(L) dissociates the homodimers and triggers Bcl-x(L) binding to mitochondrial membranes. The C-terminal tail of Bcl-x(L) is also required to mediate Bcl-x(L)/Bax heterodimer formation. Both mitochondrial import and antiapoptotic activity of different Bcl-x(L) mutants correlate with their ability to form homodimers.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/15131699-10049709,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15131699-10583363,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15131699-10791976,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15131699-11106734,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15131699-11136736,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15131699-11206074,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15131699-11326099,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15131699-11423909,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15131699-11526448,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15131699-11583631,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15131699-11983156,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15131699-12209154,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15131699-12242151,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15131699-12515824,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15131699-12651847,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15131699-12660157,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15131699-12721291,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15131699-12783855,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15131699-12831534,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15131699-12952938,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15131699-14499110,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15131699-7068762,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15131699-7644501,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15131699-8159715,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15131699-8358790,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15131699-8929527,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15131699-9020082,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15131699-9027314,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15131699-9108035,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15131699-9153240,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15131699-9553144,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15131699-9735050,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15131699-9742125,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15131699-9927423
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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/BAD protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/BAX protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/BCL2L1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Bax protein (53-86),
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-bcl-2,
http://linkedlifedata.com/resource/pubmed/chemical/bcl-2-Associated X Protein,
http://linkedlifedata.com/resource/pubmed/chemical/bcl-Associated Death Protein,
http://linkedlifedata.com/resource/pubmed/chemical/bcl-X Protein
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0261-4189
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
19
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pubmed:volume |
23
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2146-55
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:15131699-Amino Acid Sequence,
pubmed-meshheading:15131699-Animals,
pubmed-meshheading:15131699-Apoptosis,
pubmed-meshheading:15131699-Binding Sites,
pubmed-meshheading:15131699-Carrier Proteins,
pubmed-meshheading:15131699-Cell Line,
pubmed-meshheading:15131699-Cytoplasm,
pubmed-meshheading:15131699-Dimerization,
pubmed-meshheading:15131699-Humans,
pubmed-meshheading:15131699-Mitochondria,
pubmed-meshheading:15131699-Molecular Sequence Data,
pubmed-meshheading:15131699-Mutation,
pubmed-meshheading:15131699-Peptide Fragments,
pubmed-meshheading:15131699-Protein Binding,
pubmed-meshheading:15131699-Protein Structure, Quaternary,
pubmed-meshheading:15131699-Protein Structure, Secondary,
pubmed-meshheading:15131699-Proto-Oncogene Proteins,
pubmed-meshheading:15131699-Proto-Oncogene Proteins c-bcl-2,
pubmed-meshheading:15131699-Sequence Alignment,
pubmed-meshheading:15131699-bcl-2-Associated X Protein,
pubmed-meshheading:15131699-bcl-Associated Death Protein,
pubmed-meshheading:15131699-bcl-X Protein
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pubmed:year |
2004
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pubmed:articleTitle |
Bcl-x(L) sequesters its C-terminal membrane anchor in soluble, cytosolic homodimers.
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pubmed:affiliation |
Biochemistry Section, Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892-1414, USA.
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