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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2001-2-8
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pubmed:abstractText |
The interaction of the anti-apoptotic members of the Bcl-2 family with mitochondria, through their hydrophobic C-terminus, has been proposed to play a crucial role in the execution phase of apoptosis. We report here that a substitution of the C-terminal end of pro-apoptotic bax by that of anti-apoptotic bcl-xL (baxCxL) does not modify its association with mitochondria in human and rat cells or in Saccharomyces cerevisiae. In addition, while bax sensitizes these cells to apoptotic stimuli, the construct baxCxL does not affect the apoptotic response in transfected cells. These results suggest that the C-terminus of bax plays an important role in apoptosis independently of its membrane addressing/targeting mechanism.
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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/BAX protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/BCL2L1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Bax protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Bcl2l1 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/DEVDase,
http://linkedlifedata.com/resource/pubmed/chemical/L-Lactate Dehydrogenase,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Hydrolases,
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/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/bcl-2-Associated X Protein,
http://linkedlifedata.com/resource/pubmed/chemical/bcl-X Protein
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
29
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pubmed:volume |
487
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
161-5
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11150501-Amino Acid Sequence,
pubmed-meshheading:11150501-Animals,
pubmed-meshheading:11150501-Apoptosis,
pubmed-meshheading:11150501-Cell Membrane,
pubmed-meshheading:11150501-Cytosol,
pubmed-meshheading:11150501-Glioma,
pubmed-meshheading:11150501-Humans,
pubmed-meshheading:11150501-K562 Cells,
pubmed-meshheading:11150501-L-Lactate Dehydrogenase,
pubmed-meshheading:11150501-Mitochondria,
pubmed-meshheading:11150501-Molecular Sequence Data,
pubmed-meshheading:11150501-Peptide Hydrolases,
pubmed-meshheading:11150501-Proto-Oncogene Proteins,
pubmed-meshheading:11150501-Proto-Oncogene Proteins c-bcl-2,
pubmed-meshheading:11150501-Rats,
pubmed-meshheading:11150501-Recombinant Fusion Proteins,
pubmed-meshheading:11150501-Saccharomyces cerevisiae,
pubmed-meshheading:11150501-Sequence Deletion,
pubmed-meshheading:11150501-Transfection,
pubmed-meshheading:11150501-Tumor Cells, Cultured,
pubmed-meshheading:11150501-Ultraviolet Rays,
pubmed-meshheading:11150501-bcl-2-Associated X Protein,
pubmed-meshheading:11150501-bcl-X Protein
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pubmed:year |
2000
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pubmed:articleTitle |
The substitution of the C-terminus of bax by that of bcl-xL does not affect its subcellular localization but abrogates its pro-apoptotic properties.
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pubmed:affiliation |
Unité INSERM 419, Nantes Cedex 1, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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