rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5182
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pubmed:dateCreated |
1994-11-8
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pubmed:abstractText |
In this study, a protein that interacts with sequences encoded by the first exon of the protein kinase Bcr was cloned. The Bcr-associated protein 1 (Bap-1) is a member of the 14-3-3 family of proteins. Bap-1 interacts with full-length c-Bcr and with the chimeric Bcr-Abl tyrosine kinase of Philadelphia chromosome (Ph1)-positive human leukemias. Bap-1 is a substrate for the Bcr serine-threonine kinase and is also phosphorylated on tyrosine by Bcr-Abl but not by c-Abl. Bap-1 may function in the regulation of c-Bcr and may contribute to the transforming activity of Bcr-Abl in vivo. 14-3-3 proteins are essential for cell proliferation and have a role in determining the timing of mitosis in yeast. Through direct binding to sequences present in Bcr and in other proteins implicated in signaling, the mammalian 14-3-3 proteins may link specific signaling protein components to mitogenic and cell-cycle control pathways.
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pubmed:grant |
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pubmed:commentsCorrections |
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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/14-3-3 Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/BCR protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Bcr protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Fusion Proteins, bcr-abl,
http://linkedlifedata.com/resource/pubmed/chemical/Poly(ADP-ribose) Polymerases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-bcr,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine 3-Monooxygenase
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0036-8075
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
7
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pubmed:volume |
266
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
129-33
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:7939633-14-3-3 Proteins,
pubmed-meshheading:7939633-Animals,
pubmed-meshheading:7939633-Cell Division,
pubmed-meshheading:7939633-Cell Line,
pubmed-meshheading:7939633-Cell Transformation, Neoplastic,
pubmed-meshheading:7939633-Fusion Proteins, bcr-abl,
pubmed-meshheading:7939633-Humans,
pubmed-meshheading:7939633-Mice,
pubmed-meshheading:7939633-Phosphorylation,
pubmed-meshheading:7939633-Poly(ADP-ribose) Polymerases,
pubmed-meshheading:7939633-Protein-Tyrosine Kinases,
pubmed-meshheading:7939633-Proteins,
pubmed-meshheading:7939633-Proto-Oncogene Proteins,
pubmed-meshheading:7939633-Proto-Oncogene Proteins c-bcr,
pubmed-meshheading:7939633-Rats,
pubmed-meshheading:7939633-Recombinant Fusion Proteins,
pubmed-meshheading:7939633-Signal Transduction,
pubmed-meshheading:7939633-Tyrosine 3-Monooxygenase
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pubmed:year |
1994
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pubmed:articleTitle |
Association of the protein kinases c-Bcr and Bcr-Abl with proteins of the 14-3-3 family.
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pubmed:affiliation |
Department of Pharmacology, Duke University Medical Center, Durham, NC 27710.
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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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