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Details on Person Tyrosine phosphorylateion is believed to be a general activa...
| Class:Id | Summation:437949 |
|---|---|
| _displayName | Tyrosine phosphorylateion is believed to be a general activa... |
| _timestamp | 2010-06-02 14:35:09 |
| created | [InstanceEdit:437933] Jupe, S, 2009-09-18 |
| literatureReference | [LiteratureReference:437937] Structural basis for relief of autoinhibition of the Dbl homology domain of proto-oncogene Vav by tyrosine phosphorylation [LiteratureReference:430169] Vav2 activates c-fos serum response element and CD69 expression but negatively regulates nuclear factor of activated T cells and interleukin-2 gene activation in T lymphocyte [LiteratureReference:870195] Vav family proteins are required for optimal regulation of PLCgamma2 by integrin alphaIIbbeta3 |
| modified | [InstanceEdit:442288] Jupe, S, 2009-09-24 [InstanceEdit:870198] Jupe, S, 2010-06-02 |
| text | Tyrosine phosphorylateion is believed to be a general activation mechansim for the Vav family. VAV1 Tyr-174 binds to the Dbl homology region, inhibiting GEF activity. Phosphorylation of this residue by Syk relieves inhibition, activating Vav1. In Jurkat cells T-cell receptor activation leads to increased Vav2 tyrosine phosphorylation; the expression of Lck, Fyn, Zap70, or Syk stimulated this phosphorylation. Vav is regulated downstream of the thrombin and thrombopoietin receptors (Miyakawa et al. 1997) and integrins, including the major platelet integrin alphaIIbbeta3. Vav family proteins are involved in filopodia and lamellipodia formation; mouse platelets deficient in Vav1 and Vav3 exhibit reduced filopodia and lamellipodia formation during spreading on fibrinogen. This is accompanied by reduced alphaIIbbeta3-mediated PLCgamma2 tyrosine phosphorylation and reduced Ca(2+) mobilization (Pearce et al. 2007). |
| (summation) | [Reaction:437936] p-Y348-SYK phosphorylates VAV family [Homo sapiens] [Reaction:437938] Syk phosphorylates VAV1 [Homo sapiens] |
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