Article
The tyrosine phosphorylated carboxyterminus of the EGF receptor is a binding site for GAP and PLC-gamma.
The EMBO journal - 1 Dec 1990
Margolis B, Li N, Koch A, Mohammadi M, Hurwitz D R, Zilberstein A, Ullrich A, Pawson T, Schlessinger J
Abstract excerpt
Phospholipase C-gamma (PLC-gamma) and GTPase activating protein (GAP) are substrates of EGF, PDGF and other growth factor receptors. Since either PLC-gamma or GAP also bind to the activated receptors it was suggested that their SH2 domains are mediating this association. We attempted to delineate...
Topics
- Animals
- Binding Sites
- Cell Line
- ErbB Receptors
- GTPase-Activating Proteins
- Mice
- Mice, Inbred Strains
- Mutation
- Phosphatidylinositol Diacylglycerol-Lyase
- Phosphoric Diester Hydrolases
- Phosphorylation
- Proteins
- Recombinant Fusion Proteins
- Tyrosine