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Details on Person The activity of Src-kinase is increased when bound to Beta-a...
| Class:Id | Summation:418157 |
|---|---|
| _displayName | The activity of Src-kinase is increased when bound to Beta-a... |
| _timestamp | 2020-12-02 14:22:52 |
| created | [InstanceEdit:418159] Jupe, S, 2009-04-16 13:03:44 |
| literatureReference | [LiteratureReference:418153] Beta-arrestin-dependent formation of beta2 adrenergic receptor-Src protein kinase complexes [LiteratureReference:418092] Opposing effects of beta-arrestin1 and beta-arrestin2 on activation and degradation of Src induced by protease-activated receptor 1 |
| modified | [InstanceEdit:9708864] Jassal, Bijay, 2020-12-02 |
| text | The activity of Src-kinase is increased when bound to Beta-arrestin-1. The mechanism for this activation is not clear. Src bound to beta -arrestin 1 is substantially dephosphorylated at Tyr530 and this is often associated with Src activation. Binding results with Y530F mutants of Src suggest that binding of Src to arrestin causes a conformational activation of the kinase, rather than a change in phosphorylation. However, increased phosphorylation of Src Tyr419 in cells overexpressing beta-arrestin-1 has been reported to correlate with PAR1 activation, beta-arrestin signalling complex formation, and increased ERK activation. |
| (summation) | [BlackBoxEvent:418158] SRC-1 is activated (in F2R:ARRB1:MAPKs:SRC-1) [Homo sapiens] |
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