Source:http://www.reactome.org/biopax/48887BiochemicalReaction1776
| Predicate | Object |
|---|---|
| rdf:type | |
| biopax3:comment |
Authored: de Bono, B, 2007-01-10 10:27:18,
Edited: Jupe, S, 2010-02-03,
Recruitment of PLC-gamma by FGF receptors has been best studied in FGFR1c signaling, where it has been shown that autophosphorylation of Tyr766 in the C-terminal tail of FGFR1c creates a specific binding site for the SH2 domain of PLC-gamma. A mutant FGFR1c in which Y766 is replaced by phenylalanine is unable to activate PI hydrolysis and Ca2+ release in response to FGF stimulation. Membrane recruitment of PLC-gamma is also aided by binding of the Pleckstrin homology (PH) domain of this enzyme to PtIns(3,4,5) P3 molecules that are generated in response to PI-3 kinase stimulation. By sequence comparison, Y766 is conserved in all FGFR isoforms, and PLC-gamma signaling is observed, to a greater or lesser extent, downstream of all FGFR receptors upon stimulation with FGFs.,
Reviewed: Mohammadi, M, 2007-02-06 21:44:35
|
| biopax3:xref | |
| biopax3:dataSource | |
| biopax3:displayName |
Activated FGFR binds PLC-gamma
|
| biopax3:left | |
| biopax3:right |