| pubmed-article:9804835 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9804835 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
| pubmed-article:9804835 | lifeskim:mentions | umls-concept:C0034789 | lld:lifeskim |
| pubmed-article:9804835 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:9804835 | lifeskim:mentions | umls-concept:C0037083 | lld:lifeskim |
| pubmed-article:9804835 | lifeskim:mentions | umls-concept:C1522290 | lld:lifeskim |
| pubmed-article:9804835 | lifeskim:mentions | umls-concept:C1414900 | lld:lifeskim |
| pubmed-article:9804835 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
| pubmed-article:9804835 | lifeskim:mentions | umls-concept:C0439064 | lld:lifeskim |
| pubmed-article:9804835 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
| pubmed-article:9804835 | pubmed:issue | 46 | lld:pubmed |
| pubmed-article:9804835 | pubmed:dateCreated | 1998-12-8 | lld:pubmed |
| pubmed-article:9804835 | pubmed:abstractText | Gab1 is a member of the docking/scaffolding protein family which includes IRS-1, IRS-2, c-Cbl, p130(cas), and p62(dok). These proteins contain a variety of protein-protein interaction motifs including multiple tyrosine residues that when phosphorylated can act as binding sites for Src homology 2 (SH2) domain-containing signaling proteins. We show in the RAMOS human B cell line that Gab1 is tyrosine-phosphorylated in response to B cell antigen receptor (BCR) engagement. Moreover, tyrosine phosphorylation of Gab1 correlated with the binding of several SH2-containing signaling proteins to Gab1 including Shc, Grb2, phosphatidylinositol 3-kinase, and the SHP-2 tyrosine phosphatase. Far Western analysis showed that the SH2 domains of Shc, SHP-2, and the p85 subunit of phosphatidylinositol 3-kinase could bind directly to tyrosine-phosphorylated Gab1 isolated from activated RAMOS cells. In contrast, the Grb2 SH2 domain did not bind directly to Gab1 but instead to the Shc and SHP-2 associated with Gab1. We also show that Gab1 is present in the membrane-enriched particulate fraction of RAMOS cells and that Gab1/signaling protein complexes are found in this fraction after BCR engagement. Thus, tyrosine-phosphorylated Gab1 may recruit cytosolic signaling proteins to cellular membranes where they can act on membrane-bound targets. This may be a critical step in the activation of multiple BCR signaling pathways. | lld:pubmed |
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| pubmed-article:9804835 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:9804835 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9804835 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9804835 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:9804835 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:9804835 | pubmed:author | pubmed-author:SilJJ | lld:pubmed |
| pubmed-article:9804835 | pubmed:author | pubmed-author:InghamR JRJ | lld:pubmed |
| pubmed-article:9804835 | pubmed:author | pubmed-author:GoldM RMR | lld:pubmed |
| pubmed-article:9804835 | pubmed:author | pubmed-author:WongA JAJ | lld:pubmed |
| pubmed-article:9804835 | pubmed:author | pubmed-author:Holgado-Madru... | lld:pubmed |
| pubmed-article:9804835 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9804835 | pubmed:day | 13 | lld:pubmed |
| pubmed-article:9804835 | pubmed:volume | 273 | lld:pubmed |
| pubmed-article:9804835 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9804835 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9804835 | pubmed:pagination | 30630-7 | lld:pubmed |
| pubmed-article:9804835 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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| pubmed-article:9804835 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9804835 | pubmed:articleTitle | The Gab1 protein is a docking site for multiple proteins involved in signaling by the B cell antigen receptor. | lld:pubmed |
| pubmed-article:9804835 | pubmed:affiliation | Department of Microbiology and Immunology, University of British Columbia, Vancouver, British Columbia V6T 1Z3, Canada. | lld:pubmed |
| pubmed-article:9804835 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9804835 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:9804835 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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