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rdf:type |
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lifeskim:mentions |
umls-concept:C0004083,
umls-concept:C0044602,
umls-concept:C0439851,
umls-concept:C1333707,
umls-concept:C1418576,
umls-concept:C1418577,
umls-concept:C1423080,
umls-concept:C1423613,
umls-concept:C1552596,
umls-concept:C1711351,
umls-concept:C1947931
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pubmed:issue |
21
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pubmed:dateCreated |
1995-6-28
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pubmed:abstractText |
Phosphatidylinositol 3-kinase (PI 3-kinase) has been shown to play a key role in growth factor signaling pathways, although its signaling mechanism has not been fully elucidated. Using the yeast interaction trap system, we have identified Grb2 as a PI 3-kinase interacting protein. Our experiments demonstrate that p85, the regulatory subunit of PI 3-kinase, interacts with Grb2 in vivo, and this interaction is independent of growth factor stimulation. The direct association between Grb2 and p85 was reconstituted in vitro with glutathione S-transferase fusion proteins. Domain analyses and peptide competition indicate that the association is mediated by the SH3 domains of Grb2 and the proline-rich motifs of p85 and that only one SH3 domain is required for minimal binding. The interaction does not displace the catalytic subunit of PI 3-kinase but is exclusive of Sos. Signaling through PI 3-kinase, therefore, may involve the ubiquitous adapter Grb2, which serves as a convergence point for multiple pathways.
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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/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/GRB2 Adaptor Protein,
http://linkedlifedata.com/resource/pubmed/chemical/GRB2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Grb2 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol 3-Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphotransferases (Alcohol Group...,
http://linkedlifedata.com/resource/pubmed/chemical/Platelet-Derived Growth Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
26
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pubmed:volume |
270
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
12774-80
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:7759531-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:7759531-Amino Acid Sequence,
pubmed-meshheading:7759531-Animals,
pubmed-meshheading:7759531-Base Sequence,
pubmed-meshheading:7759531-Cattle,
pubmed-meshheading:7759531-Cells, Cultured,
pubmed-meshheading:7759531-DNA, Complementary,
pubmed-meshheading:7759531-Escherichia coli,
pubmed-meshheading:7759531-GRB2 Adaptor Protein,
pubmed-meshheading:7759531-Gene Library,
pubmed-meshheading:7759531-Humans,
pubmed-meshheading:7759531-Molecular Sequence Data,
pubmed-meshheading:7759531-Phosphatidylinositol 3-Kinases,
pubmed-meshheading:7759531-Phosphotransferases (Alcohol Group Acceptor),
pubmed-meshheading:7759531-Platelet-Derived Growth Factor,
pubmed-meshheading:7759531-Precipitin Tests,
pubmed-meshheading:7759531-Protein Binding,
pubmed-meshheading:7759531-Protein Conformation,
pubmed-meshheading:7759531-Proteins,
pubmed-meshheading:7759531-Rats,
pubmed-meshheading:7759531-Recombinant Fusion Proteins,
pubmed-meshheading:7759531-Selection, Genetic,
pubmed-meshheading:7759531-Sequence Analysis, DNA,
pubmed-meshheading:7759531-Signal Transduction,
pubmed-meshheading:7759531-Yeasts
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pubmed:year |
1995
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pubmed:articleTitle |
Direct association of Grb2 with the p85 subunit of phosphatidylinositol 3-kinase.
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pubmed:affiliation |
Division of Cell and Molecular Biology, Dana-Farber Cancer Institute, Boston, Massachusetts, USA.
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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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