| pubmed-article:7522233 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7522233 | lifeskim:mentions | umls-concept:C0021758 | lld:lifeskim |
| pubmed-article:7522233 | lifeskim:mentions | umls-concept:C0079784 | lld:lifeskim |
| pubmed-article:7522233 | lifeskim:mentions | umls-concept:C0018183 | lld:lifeskim |
| pubmed-article:7522233 | lifeskim:mentions | umls-concept:C0021764 | lld:lifeskim |
| pubmed-article:7522233 | lifeskim:mentions | umls-concept:C0031621 | lld:lifeskim |
| pubmed-article:7522233 | lifeskim:mentions | umls-concept:C0656342 | lld:lifeskim |
| pubmed-article:7522233 | lifeskim:mentions | umls-concept:C1519726 | lld:lifeskim |
| pubmed-article:7522233 | lifeskim:mentions | umls-concept:C1333707 | lld:lifeskim |
| pubmed-article:7522233 | lifeskim:mentions | umls-concept:C0004083 | lld:lifeskim |
| pubmed-article:7522233 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
| pubmed-article:7522233 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:7522233 | pubmed:issue | 38 | lld:pubmed |
| pubmed-article:7522233 | pubmed:dateCreated | 1994-10-20 | lld:pubmed |
| pubmed-article:7522233 | 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. | lld:pubmed |
| pubmed-article:7522233 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:7522233 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:7522233 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7522233 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:7522233 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:7522233 | pubmed:author | pubmed-author:SchraderJ WJW | lld:pubmed |
| pubmed-article:7522233 | pubmed:author | pubmed-author:WelhamM JMJ | lld:pubmed |
| pubmed-article:7522233 | pubmed:author | pubmed-author:LeslieK BKB | lld:pubmed |
| pubmed-article:7522233 | pubmed:author | pubmed-author:JirikFF | lld:pubmed |
| pubmed-article:7522233 | pubmed:author | pubmed-author:DechertUU | lld:pubmed |
| pubmed-article:7522233 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7522233 | pubmed:day | 23 | lld:pubmed |
| pubmed-article:7522233 | pubmed:volume | 269 | lld:pubmed |
| pubmed-article:7522233 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7522233 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7522233 | pubmed:pagination | 23764-8 | lld:pubmed |
| pubmed-article:7522233 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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| pubmed-article:7522233 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:7522233 | 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. | lld:pubmed |
| pubmed-article:7522233 | pubmed:affiliation | Biomedical Research Centre, University of British Columbia, Vancouver, Canada. | lld:pubmed |
| pubmed-article:7522233 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7522233 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:7522233 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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