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• W1807220775 startingPage "4749" @default.
• W1807220775 abstract "We recently identified Vav as a Ras-activating guanine nucleotide exchange factor (GEF) stimulated by a T-cell antigen receptor-coupled protein tyrosine kinase (PTK). Here, we describe a novel, protein kinase-independent alternative pathway of Vav activation. Phorbol ester, 1,2-diacylglycerol, or ceramide treatment of intact T cells, Vav immunoprecipitates, or partially purified Vav generated by in vitro translation or COS-1 cell transfection stimulated the Ras exchange activity of Vav in the absence of detectable tyrosine phosphorylation. GEF activity of gel-purified Vav was similarly stimulated by phorbol myristate acetate (PMA). Stimulation was resistant to PTK and protein kinase C inhibitors but was blocked by calphostin, a PMA and diacylglycerol antagonist. In vitro-translated Vav lacking its cysteine-rich domain, or mutated at a single cysteine residue within this domain (C528A), was not stimulated by PMA but was fully activated by p56lck. This correlated with increased binding of radiolabeled phorbol ester to COS-1 cells expressing wild-type, but not C528A-mutated, Vav. Thus, Vav itself is a PMA-binding and -activated Ras GEF. Recombinant interleukin-1 alpha stimulated Vav via this pathway, suggesting that diglyceride-mediated Vav activation may couple PTK-independent receptors which stimulate production of lipid second messengers to Ras in hematopoietic cells." @default.
• W1807220775 created "2016-06-24" @default.
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• W1807220775 date "1994-07-01" @default.
• W1807220775 modified "2023-10-18" @default.
• W1807220775 title "Direct stimulation of Vav guanine nucleotide exchange activity for Ras by phorbol esters and diglycerides" @default.
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• W1807220775 doi "https://doi.org/10.1128/mcb.14.7.4749-4758.1994" @default.
• W1807220775 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/358848" @default.
• W1807220775 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/7516472" @default.
• W1807220775 hasPublicationYear "1994" @default.
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