pubmed-article:7642581 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:7642581 | lifeskim:mentions | umls-concept:C0044602 | lld:lifeskim |
pubmed-article:7642581 | lifeskim:mentions | umls-concept:C0039194 | lld:lifeskim |
pubmed-article:7642581 | lifeskim:mentions | umls-concept:C0031689 | lld:lifeskim |
pubmed-article:7642581 | lifeskim:mentions | umls-concept:C0033713 | lld:lifeskim |
pubmed-article:7642581 | lifeskim:mentions | umls-concept:C1333707 | lld:lifeskim |
pubmed-article:7642581 | lifeskim:mentions | umls-concept:C1417754 | lld:lifeskim |
pubmed-article:7642581 | lifeskim:mentions | umls-concept:C2003939 | lld:lifeskim |
pubmed-article:7642581 | lifeskim:mentions | umls-concept:C1704241 | lld:lifeskim |
pubmed-article:7642581 | lifeskim:mentions | umls-concept:C1514468 | lld:lifeskim |
pubmed-article:7642581 | lifeskim:mentions | umls-concept:C1515655 | lld:lifeskim |
pubmed-article:7642581 | pubmed:issue | 32 | lld:pubmed |
pubmed-article:7642581 | pubmed:dateCreated | 1995-9-18 | lld:pubmed |
pubmed-article:7642581 | pubmed:abstractText | Previously, we have identified p120 as a Fyn/Lck SH3 and SH2 domain-binding protein that is tyrosine phosphorylated rapidly after T cell receptor triggering. Here, we used direct protein purification, amino acid sequence analysis, reactivity with antibodies, and two-dimensional gel analyses to identify p120 as the human c-cbl protooncogene product. We demonstrate in vivo complexes of p120cbl with Fyn tyrosine kinase, the adaptor protein Grb2, and the p85 subunit of phosphatidylinositol (PI) 3-kinase. The association of p120cbl with Fyn and the p85 subunit of PI 3-kinase (together with PI 3-kinase activity) was markedly increased by T cell activation, consistent with in vitro binding of p120cbl to their SH2 as well as SH3 domains. In contrast, a large fraction of p120cbl was associated with Grb2 prior to activation, and this association did not change upon T cell activation. In vitro, p120cbl interacted with Grb2 exclusively through its SH3 domains. These results demonstrate a novel Grb2-p120cbl signaling complex in T cells, distinct from the previously analyzed Grb2-Sos complex. The association of p120cbl with ubiquitous signaling proteins strongly suggests a general signal transducing function for this enigmatic protooncogene with established leukemogenic potential but unknown physiological function. | lld:pubmed |
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pubmed-article:7642581 | pubmed:language | eng | lld:pubmed |
pubmed-article:7642581 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7642581 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:7642581 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:7642581 | pubmed:month | Aug | lld:pubmed |
pubmed-article:7642581 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:7642581 | pubmed:author | pubmed-author:SoltoffSS | lld:pubmed |
pubmed-article:7642581 | pubmed:author | pubmed-author:FukazawaTT | lld:pubmed |
pubmed-article:7642581 | pubmed:author | pubmed-author:BaniGG | lld:pubmed |
pubmed-article:7642581 | pubmed:author | pubmed-author:DrukerBB | lld:pubmed |
pubmed-article:7642581 | pubmed:author | pubmed-author:ShoelsonS ESE | lld:pubmed |
pubmed-article:7642581 | pubmed:author | pubmed-author:Panchamoorthy... | lld:pubmed |
pubmed-article:7642581 | pubmed:author | pubmed-author:CantleyLL | lld:pubmed |
pubmed-article:7642581 | pubmed:author | pubmed-author:ReedquistK... | lld:pubmed |
pubmed-article:7642581 | pubmed:author | pubmed-author:SHIMS SSS | lld:pubmed |
pubmed-article:7642581 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:7642581 | pubmed:day | 11 | lld:pubmed |
pubmed-article:7642581 | pubmed:volume | 270 | lld:pubmed |
pubmed-article:7642581 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:7642581 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:7642581 | pubmed:pagination | 19141-50 | lld:pubmed |
pubmed-article:7642581 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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pubmed-article:7642581 | pubmed:year | 1995 | lld:pubmed |
pubmed-article:7642581 | pubmed:articleTitle | The SH3 domain-binding T cell tyrosyl phosphoprotein p120. Demonstration of its identity with the c-cbl protooncogene product and in vivo complexes with Fyn, Grb2, and phosphatidylinositol 3-kinase. | lld:pubmed |
pubmed-article:7642581 | pubmed:affiliation | Department of Rheumatology and Immunology, Brigham and Women's Hospital, Boston, Massachusetts 02115, USA. | lld:pubmed |
pubmed-article:7642581 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:7642581 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:7642581 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
pubmed-article:7642581 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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