| pubmed-article:8621719 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8621719 | lifeskim:mentions | umls-concept:C0044602 | lld:lifeskim |
| pubmed-article:8621719 | lifeskim:mentions | umls-concept:C0034789 | lld:lifeskim |
| pubmed-article:8621719 | lifeskim:mentions | umls-concept:C0033681 | lld:lifeskim |
| pubmed-article:8621719 | lifeskim:mentions | umls-concept:C1519726 | lld:lifeskim |
| pubmed-article:8621719 | lifeskim:mentions | umls-concept:C1333707 | lld:lifeskim |
| pubmed-article:8621719 | lifeskim:mentions | umls-concept:C1418576 | lld:lifeskim |
| pubmed-article:8621719 | lifeskim:mentions | umls-concept:C1418577 | lld:lifeskim |
| pubmed-article:8621719 | lifeskim:mentions | umls-concept:C1423080 | lld:lifeskim |
| pubmed-article:8621719 | lifeskim:mentions | umls-concept:C1423613 | lld:lifeskim |
| pubmed-article:8621719 | lifeskim:mentions | umls-concept:C1948023 | lld:lifeskim |
| pubmed-article:8621719 | lifeskim:mentions | umls-concept:C1710236 | lld:lifeskim |
| pubmed-article:8621719 | lifeskim:mentions | umls-concept:C0205164 | lld:lifeskim |
| pubmed-article:8621719 | lifeskim:mentions | umls-concept:C1515655 | lld:lifeskim |
| pubmed-article:8621719 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
| pubmed-article:8621719 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:8621719 | pubmed:dateCreated | 1996-6-19 | lld:pubmed |
| pubmed-article:8621719 | pubmed:abstractText | We and others have demonstrated that the c-cbl proto-oncogene product is one of the earliest targets of tyrosine phosphorylation upon T cell receptor stimulation. Given the similarities in the B and T lymphocyte antigen receptors, and the induction of pre-B leukemias in mice by the v-cbl oncogene, we examined the potential involvement of Cbl in B cell receptor signaling. We demonstrate prominent and early tyrosine phosphorylation of Cbl upon stimulation of human B cell lines through surface IgM. Cbl was associated in vivo with Fyn and, to a lesser extent, other Src family kinases. B cell activation also induced a prominent association of Cbl with Syk tyrosine kinase. A substantial fraction of Cbl was constitutively associated with Grb2 and this interaction was mediated by Grb2 SH3 domains. Tyrosine-phosphorylated Shc, which prominently associated with Grb2, was detected in association with Cbl in activated B cells. Thus, Grb2 and Shc adaptors, which associate with immunoreceptor tyrosine based activation motifs, may link Cbl to the B cell receptor. B cell activation also induced a prominent association between Cbl and the p85 subunit of phosphatidylinositol (PI) 3-kinase resulting in the association of a substantial fraction of PI 3-kinase activity with Cbl. Thus, Cbl is likely to play an important role to couple the B cell receptor to the PI 3-kinase pathway. Our results strongly suggest a role for p120cbl in signaling downstream of the B cell receptor and support the idea that Cbl participates in a general signal transduction function downstream of the immune cell surface receptors. | lld:pubmed |
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| pubmed-article:8621719 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:8621719 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8621719 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:8621719 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:8621719 | pubmed:author | pubmed-author:SoltoffSS | lld:pubmed |
| pubmed-article:8621719 | pubmed:author | pubmed-author:MiyakeSS | lld:pubmed |
| pubmed-article:8621719 | pubmed:author | pubmed-author:FukazawaTT | lld:pubmed |
| pubmed-article:8621719 | pubmed:author | pubmed-author:BaniGG | lld:pubmed |
| pubmed-article:8621719 | pubmed:author | pubmed-author:DrukerBB | lld:pubmed |
| pubmed-article:8621719 | pubmed:author | pubmed-author:ShoelsonSS | lld:pubmed |
| pubmed-article:8621719 | pubmed:author | pubmed-author:Panchamoorthy... | lld:pubmed |
| pubmed-article:8621719 | pubmed:author | pubmed-author:CantleyLL | lld:pubmed |
| pubmed-article:8621719 | pubmed:author | pubmed-author:ReedquistKK | lld:pubmed |
| pubmed-article:8621719 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8621719 | pubmed:day | 9 | lld:pubmed |
| pubmed-article:8621719 | pubmed:volume | 271 | lld:pubmed |
| pubmed-article:8621719 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8621719 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8621719 | pubmed:pagination | 3187-94 | lld:pubmed |
| pubmed-article:8621719 | pubmed:dateRevised | 2011-11-2 | lld:pubmed |
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| pubmed-article:8621719 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8621719 | pubmed:articleTitle | p120cbl is a major substrate of tyrosine phosphorylation upon B cell antigen receptor stimulation and interacts in vivo with Fyn and Syk tyrosine kinases, Grb2 and Shc adaptors, and the p85 subunit of phosphatidylinositol 3-kinase. | lld:pubmed |
| pubmed-article:8621719 | pubmed:affiliation | Lymphocyte Biology Section, Division of Rheumatology and Immunology, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts 02115, USA. | lld:pubmed |
| pubmed-article:8621719 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8621719 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8621719 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:8621719 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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