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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
11
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pubmed:dateCreated |
1997-10-30
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pubmed:abstractText |
Sam68 (Src-associated in mitosis) is an SH3 (Src-homology 3), SH2 (Src-homology 2), and RNA binding protein which associates with and is tyrosine phosphorylated by wild-type and activated forms of c-Src in a mitosis-specific manner. We now show that Sam68 immunoprecipitated from either HeLa S3 or NIH3T3 cells is phosphorylated on threonine residues exclusively during mitosis as well as on serine residues during both interphase and mitosis. Recombinant Sam68, expressed as a glutathione S-transferase (GST) fusion protein, was phosphorylated on threonine and serine residues after incubation with mitotic lysates several-fold more extensively than after incubation with unsynchronized lysates. Cdc2 was identified as the kinase responsible for the mitotic threonine phosphorylation by (1) immunodepletion of the mitotic Sam68 kinase from cell lysates with anti-Cdc2 antibodies, (2) inhibition of Sam68 phosphorylation in vitro and in vivo by the cyclin-dependent kinase inhibitor olomoucine and (3) phosphorylation of Sam68 by purified Cdc2. These data demonstrate that Sam68 is a direct target of Cdc2 and may therefore mediate some of its biological effects during mitosis.
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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/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/CDC2 Protein Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Extracts,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclin B,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/KHDRBS1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Khdrbs1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Kinetin,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins pp60(c-src),
http://linkedlifedata.com/resource/pubmed/chemical/Purines,
http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Serine,
http://linkedlifedata.com/resource/pubmed/chemical/Threonine,
http://linkedlifedata.com/resource/pubmed/chemical/olomoucine
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0950-9232
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
15
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1247-53
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:9315091-3T3 Cells,
pubmed-meshheading:9315091-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:9315091-Animals,
pubmed-meshheading:9315091-CDC2 Protein Kinase,
pubmed-meshheading:9315091-Cell Cycle,
pubmed-meshheading:9315091-Cell Extracts,
pubmed-meshheading:9315091-Cyclin B,
pubmed-meshheading:9315091-DNA-Binding Proteins,
pubmed-meshheading:9315091-Enzyme Inhibitors,
pubmed-meshheading:9315091-HeLa Cells,
pubmed-meshheading:9315091-Humans,
pubmed-meshheading:9315091-Interphase,
pubmed-meshheading:9315091-Kinetin,
pubmed-meshheading:9315091-Mice,
pubmed-meshheading:9315091-Mitosis,
pubmed-meshheading:9315091-Phosphorylation,
pubmed-meshheading:9315091-Proto-Oncogene Proteins pp60(c-src),
pubmed-meshheading:9315091-Purines,
pubmed-meshheading:9315091-RNA-Binding Proteins,
pubmed-meshheading:9315091-Recombinant Proteins,
pubmed-meshheading:9315091-Serine,
pubmed-meshheading:9315091-Threonine
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pubmed:year |
1997
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pubmed:articleTitle |
Phosphorylation of the Src substrate Sam68 by Cdc2 during mitosis.
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pubmed:affiliation |
Section of Biochemistry, Molecular and Cell Biology, Cornell University, Ithaca, NY 14853, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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