Binding of GAP to Activated PDGF Receptors
- 30 March 1990
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 247 (4950) , 1578-1581
- https://doi.org/10.1126/science.2157284
Abstract
The ras proto-oncogene products appear to relay intracellular signals via the Ras guanosine triphosphatase (GTPase) activator protein, GAP. In dog epithelial cells expressing human platelet-derived growth factor (PDGF) receptors, binding of PDGF caused approximately one-tenth of the total GAP molecules to complex with the receptor. Studies with mutant PDGF receptors showed that maximum association required both receptor kinase activity and phosphorylatable tyrosine residues at both the identified sites of receptor autophosphorylation.This publication has 31 references indexed in Scilit:
- PDGF induction of tyrosine phosphorylation of GTPase activating proteinNature, 1989
- Genetic analysis of mammalian GAP expressed in yeastCell, 1989
- Autophosphorylation of the PDGF receptor in the kinase insert region regulates interactions with cell proteinsCell, 1989
- Identification of tyrosine‐phosphorylated colony‐stimulating factor 1 (CSF‐1) receptor and a 56‐kilodalton protein phosphorylated in intact human cells in response to CSF‐1Journal of Cellular Biochemistry, 1989
- ras GTPase activating protein: Signal transmitter and signal terminatorCell, 1989
- Protein kinase C mediates platelet-derived growth factor-induced tyrosine phosphorylation of p42.The Journal of cell biology, 1988
- Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphateNature, 1988
- The cytoplasmic protein GAP is implicated as the target for regulation by the ras gene productNature, 1988
- ras GENESAnnual Review of Biochemistry, 1987
- Requirement for ras proto-oncogene function during serum-stimulated growth of NIH 3T3 cellsNature, 1985