PDGF induction of tyrosine phosphorylation of GTPase activating protein
- PMID: 2480526
- DOI: 10.1038/342711a0
PDGF induction of tyrosine phosphorylation of GTPase activating protein
Abstract
The cascade of biochemical events triggered by growth factors and their receptors is central to understanding normal cell-growth regulation and its subversion in cancer. Ras proteins (p21ras) have been implicated in signal transduction pathways used by several growth factors, including platelet-derived growth factor (PDGF). These guanine nucleotide-binding Ras proteins specifically interact with a cellular GTPase-activating protein (GAP). Here we report that in intact quiescent fibroblasts, both AA and BB homodimers of PDGF rapidly induce tyrosine phosphorylation of GAP under conditions in which insulin and basic fibroblast growth factor (bFGF) are ineffective. Although GAP is located predominantly in the cytosol, most tyrosine-phosphorylated GAP is associated with the cell membrane, the site of p21ras biological activity. These results provide a direct biochemical link between activated PDGF-receptor tyrosine kinases and the p21ras-GAP mitogenic signalling system.
Similar articles
-
Activation of the colony-stimulating factor 1 receptor leads to the rapid tyrosine phosphorylation of GTPase-activating protein and activation of cellular p21ras.Oncogene. 1992 Jan;7(1):147-52. Oncogene. 1992. PMID: 1311060
-
Phosphorylation of GAP and GAP-associated proteins by transforming and mitogenic tyrosine kinases.Nature. 1990 Jan 25;343(6256):377-81. doi: 10.1038/343377a0. Nature. 1990. PMID: 1689011
-
Platelet-derived growth factor-induced p21ras-mediated signaling is independent of platelet-derived growth factor receptor interaction with GTPase-activating protein or phosphatidylinositol-3-kinase.Cell Growth Differ. 1994 Mar;5(3):341-7. Cell Growth Differ. 1994. PMID: 8018566
-
The world according to GAP.Oncogene. 1990 Sep;5(9):1281-3. Oncogene. 1990. PMID: 1699195 Review. No abstract available.
-
Interactions between p21ras proteins and their GTPase activating proteins.Cancer Surv. 1992;12:25-42. Cancer Surv. 1992. PMID: 1386285 Review.
Cited by
-
Insulin stimulation of gene expression mediated by p21ras activation.EMBO J. 1991 May;10(5):1103-9. doi: 10.1002/j.1460-2075.1991.tb08050.x. EMBO J. 1991. PMID: 2022184 Free PMC article.
-
Accumulation of p21ras.GTP in response to stimulation with epidermal growth factor and oncogene products with tyrosine kinase activity.Proc Natl Acad Sci U S A. 1990 Oct;87(20):7926-9. doi: 10.1073/pnas.87.20.7926. Proc Natl Acad Sci U S A. 1990. PMID: 2146678 Free PMC article.
-
A phosphatidylinositol-3 kinase binds to platelet-derived growth factor receptors through a specific receptor sequence containing phosphotyrosine.Mol Cell Biol. 1991 Feb;11(2):1125-32. doi: 10.1128/mcb.11.2.1125-1132.1991. Mol Cell Biol. 1991. PMID: 1703628 Free PMC article.
-
The Steel/W transduction pathway: kit autophosphorylation and its association with a unique subset of cytoplasmic signaling proteins is induced by the Steel factor.Mol Cell Biol. 1991 Jun;11(6):3043-51. doi: 10.1128/mcb.11.6.3043-3051.1991. Mol Cell Biol. 1991. PMID: 1710023 Free PMC article.
-
Suramin rapidly alters cellular tyrosine phosphorylation in prostate cancer cell lines.J Clin Invest. 1992 Dec;90(6):2166-74. doi: 10.1172/JCI116102. J Clin Invest. 1992. PMID: 1281826 Free PMC article.
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Research Materials
Miscellaneous
