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rdf:type |
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lifeskim:mentions |
umls-concept:C0004083,
umls-concept:C0018183,
umls-concept:C0021758,
umls-concept:C0021764,
umls-concept:C0031621,
umls-concept:C0079784,
umls-concept:C0205263,
umls-concept:C0656342,
umls-concept:C1333707,
umls-concept:C1519726,
umls-concept:C1879547
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pubmed:issue |
38
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pubmed:dateCreated |
1994-10-20
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pubmed:abstractText |
Binding of interleukin (IL)-3 and granulocyte/macrophage colony-stimulating factor (GM-CSF) to their high affinity cell surface receptors induces tyrosine phosphorylation of a similar set of protein substrates. We have identified one of these common substrates (p70) as the protein-tyrosine phosphatase SHPTP2. The Src homology 2 (SH2) domain of the adaptor protein Grb2 bound with high affinity to tyrosine-phosphorylated SHPTP2 following treatment of cells with IL-3 or GM-CSF, but not IL-4. This interaction was inhibited by two phosphotyrosine peptides, based on sequences within SHPTP2, which conform to the postulated consensus sequence for Grb2 SH2 recognition. Following treatment with IL-3 or GM-CSF, but not IL-4, SHPTP2 co-immunoprecipitated with antibodies directed against the p85 subunit of PI 3'-kinase. This was partially blocked by the same phosphopeptides that blocked Grb2-SH2 binding to SHPTP2. Importantly, treatment with IL-3 resulted in a 2-3-fold increase in SHPTP2 phosphatase activity. These results suggest that SHPTP2 may play an important role in integrating signals from the IL-3 and GM-CSF receptors to both Ras and PI 3'-kinase.
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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/GRB2 Adaptor Protein,
http://linkedlifedata.com/resource/pubmed/chemical/Granulocyte-Macrophage...,
http://linkedlifedata.com/resource/pubmed/chemical/Grb2 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-3,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-4,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol 3-Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphotransferases (Alcohol Group...,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphotyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatase...,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatase...,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ptpn11 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Ptpn6 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/SH2 Domain-Containing Protein...,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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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 |
23
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pubmed:volume |
269
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
23764-8
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:7522233-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:7522233-Amino Acid Sequence,
pubmed-meshheading:7522233-Animals,
pubmed-meshheading:7522233-Binding, Competitive,
pubmed-meshheading:7522233-Cells, Cultured,
pubmed-meshheading:7522233-GRB2 Adaptor Protein,
pubmed-meshheading:7522233-Granulocyte-Macrophage Colony-Stimulating Factor,
pubmed-meshheading:7522233-Interleukin-3,
pubmed-meshheading:7522233-Interleukin-4,
pubmed-meshheading:7522233-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:7522233-Mice,
pubmed-meshheading:7522233-Molecular Sequence Data,
pubmed-meshheading:7522233-Peptides,
pubmed-meshheading:7522233-Phosphatidylinositol 3-Kinases,
pubmed-meshheading:7522233-Phosphopeptides,
pubmed-meshheading:7522233-Phosphotransferases (Alcohol Group Acceptor),
pubmed-meshheading:7522233-Phosphotyrosine,
pubmed-meshheading:7522233-Protein Tyrosine Phosphatase, Non-Receptor Type 11,
pubmed-meshheading:7522233-Protein Tyrosine Phosphatase, Non-Receptor Type 6,
pubmed-meshheading:7522233-Protein Tyrosine Phosphatases,
pubmed-meshheading:7522233-Proteins,
pubmed-meshheading:7522233-SH2 Domain-Containing Protein Tyrosine Phosphatases,
pubmed-meshheading:7522233-Tyrosine
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pubmed:year |
1994
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pubmed:articleTitle |
Interleukin (IL)-3 and granulocyte/macrophage colony-stimulating factor, but not IL-4, induce tyrosine phosphorylation, activation, and association of SHPTP2 with Grb2 and phosphatidylinositol 3'-kinase.
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pubmed:affiliation |
Biomedical Research Centre, University of British Columbia, Vancouver, Canada.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
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