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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
14
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pubmed:dateCreated |
1996-8-29
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pubmed:abstractText |
The Bcl-2 protein blocks programmed cell death (apoptosis) through an unknown mechanism. Previously we identified a Bcl-2 interacting protein BAG-1 that enhances the anti-apoptotic effects of Bcl-2. Like BAG-1, the serine/threonine protein kinase Raf-1 also can functionally cooperate with Bcl-2 in suppressing apoptosis. Here we show that Raf-1 and BAG-1 specifically interact in vitro and in yeast two-hybrid assays. Raf-1 and BAG-1 can also be coimmunoprecipitated from mammalian cells and from insect cells infected with recombinant baculoviruses encoding these proteins. Furthermore, bacterially-produced BAG-1 protein can increase the kinase activity of Raf-1 in vitro. BAG-1 also activates this mammalian kinase in yeast. These observations suggest that the Bcl-2 binding protein BAG-1 joins Ras and 14-3-3 proteins as potential activators of the kinase Raf-1.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692945-1312290,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692945-1888699,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692945-2150916,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692945-2978288,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692945-7603573,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692945-7603574,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692945-7642473,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692945-7692235,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692945-7744959,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692945-7811320,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692945-7834747,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692945-7855890,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692945-7878464,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692945-7935795,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692945-7937747,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692945-7939632,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692945-7954787,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692945-8058342,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692945-8085158,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692945-8085159,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692945-8196769,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692945-8288587,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692945-8294493,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692945-8332187,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692945-8332195,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692945-8334704,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692945-8340752,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692945-8381212,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692945-8402648,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692945-8430086
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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/BCL2-associated athanogene 1 protein,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases,
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/Proto-Oncogene Proteins c-raf,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
9
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pubmed:volume |
93
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
7063-8
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:8692945-Animals,
pubmed-meshheading:8692945-Apoptosis,
pubmed-meshheading:8692945-Carrier Proteins,
pubmed-meshheading:8692945-Cercopithecus aethiops,
pubmed-meshheading:8692945-Cloning, Molecular,
pubmed-meshheading:8692945-DNA-Binding Proteins,
pubmed-meshheading:8692945-Enzyme Activation,
pubmed-meshheading:8692945-Glutathione Transferase,
pubmed-meshheading:8692945-Humans,
pubmed-meshheading:8692945-Kinetics,
pubmed-meshheading:8692945-Mammals,
pubmed-meshheading:8692945-Protein-Serine-Threonine Kinases,
pubmed-meshheading:8692945-Protein-Tyrosine Kinases,
pubmed-meshheading:8692945-Proto-Oncogene Proteins,
pubmed-meshheading:8692945-Proto-Oncogene Proteins c-bcl-2,
pubmed-meshheading:8692945-Proto-Oncogene Proteins c-raf,
pubmed-meshheading:8692945-Recombinant Fusion Proteins,
pubmed-meshheading:8692945-Saccharomyces cerevisiae,
pubmed-meshheading:8692945-Spodoptera,
pubmed-meshheading:8692945-Transcription Factors,
pubmed-meshheading:8692945-Transfection
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pubmed:year |
1996
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pubmed:articleTitle |
Bcl-2 interacting protein, BAG-1, binds to and activates the kinase Raf-1.
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pubmed:affiliation |
The Burnham Institute, La Jolla, CA 92037, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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