Reactome | Binding of Syk causes conformational changes that lead to Sy...

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created	[InstanceEdit:453180] Jupe, S, 2010-01-19
dbId	453179
displayName	Binding of Syk causes conformational changes that lead to Sy...
literatureReference	[LiteratureReference:453191] Syk activation and dissociation from the B-cell antigen receptor is mediated by phosphorylation of tyrosine 130 [LiteratureReference:453188] Molecular mechanism of the Syk activation switch [LiteratureReference:5684175] G6b-B inhibits constitutive and agonist-induced signaling by glycoprotein VI and CLEC-2
modified	[InstanceEdit:5684800] Jupe, Steve, 2015-03-23
schemaClass	Summation
text	Binding of Syk causes conformational changes that lead to Syk activation by autophosphorylation. Syk can be activated by a number of phosphorylation events, and it has been proposed that Syk may function as a switch whereby any of several possible stimuli trigger the acquisition of similar activated conformations. (Tsang et al. 2008). These phosphorylations both modulate Syk's catalytic activity (Keshvara et al. 1997) and generate docking sites for SH2 domain-containing proteins, such as c-Cbl, PLC, and Vav1. Syk tyrosine phosphorylation is reduced in the presence of the ITIM-containing immunoglobulin superfamily transmembrane protein G6B (Mori et al. 2008).

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