Association between the PDGF receptor and members of the src family of tyrosine kinases
- PMID: 1696179
- DOI: 10.1016/0092-8674(90)90013-5
Association between the PDGF receptor and members of the src family of tyrosine kinases
Abstract
We have examined the interaction between the platelet-derived growth factor (PDGF) receptor and three src family tyrosine kinases, pp60c-src, p59fyn, and pp62c-yes. The kinase activities of all three enzymes were elevated after PDGF stimulation of quiescent fibroblasts, coincident with association of the src family kinases with the PDGF receptor and other proteins. The presence of a protein of 81-85 kd in these complexes correlated with the detection of phosphatidylinositol (PI) kinase activity (previously described to associate with both the PDGF receptor and pp60c-src-middle T antigen). These results suggest that the physiological response to PDGF involves interaction of the receptor not only with serine/threonine and lipid kinases and a phospholipase, but also with other tyrosine kinases.
Similar articles
-
Association of Fyn with the activated platelet-derived growth factor receptor: requirements for binding and phosphorylation.Oncogene. 1992 Oct;7(10):1893-901. Oncogene. 1992. PMID: 1408131
-
The Src family tyrosine kinases are required for platelet-derived growth factor-mediated signal transduction in NIH 3T3 cells.Proc Natl Acad Sci U S A. 1993 Aug 15;90(16):7696-700. doi: 10.1073/pnas.90.16.7696. Proc Natl Acad Sci U S A. 1993. PMID: 8356071 Free PMC article.
-
Src family kinases are required for integrin but not PDGFR signal transduction.EMBO J. 1999 May 4;18(9):2459-71. doi: 10.1093/emboj/18.9.2459. EMBO J. 1999. PMID: 10228160 Free PMC article.
-
The p60c-src family of protein-tyrosine kinases: structure, regulation, and function.Crit Rev Oncog. 1992;3(4):401-46. Crit Rev Oncog. 1992. PMID: 1384720 Review.
-
Platelet-derived growth factor: mechanism of action and relation to oncogenes.J Cell Sci Suppl. 1985;3:65-76. doi: 10.1242/jcs.1985.supplement_3.7. J Cell Sci Suppl. 1985. PMID: 3011826 Review.
Cited by
-
Interaction of the p85 subunit of PI 3-kinase and its N-terminal SH2 domain with a PDGF receptor phosphorylation site: structural features and analysis of conformational changes.EMBO J. 1992 Dec;11(12):4261-72. doi: 10.1002/j.1460-2075.1992.tb05524.x. EMBO J. 1992. PMID: 1330535 Free PMC article.
-
Activated Src increases adhesion, survival and alpha2-integrin expression in human breast cancer cells.Biochem J. 2004 Mar 1;378(Pt 2):559-67. doi: 10.1042/BJ20031392. Biochem J. 2004. PMID: 14629195 Free PMC article.
-
Binding of the Src SH2 domain to phosphopeptides is determined by residues in both the SH2 domain and the phosphopeptides.Mol Cell Biol. 1993 Dec;13(12):7278-87. doi: 10.1128/mcb.13.12.7278-7287.1993. Mol Cell Biol. 1993. PMID: 7504171 Free PMC article.
-
Palmitoylation of p59fyn is reversible and sufficient for plasma membrane association.Mol Biol Cell. 1997 Jun;8(6):1159-73. doi: 10.1091/mbc.8.6.1159. Mol Biol Cell. 1997. PMID: 9201723 Free PMC article.
-
Csk suppression of Src involves movement of Csk to sites of Src activity.Mol Cell Biol. 1994 Aug;14(8):5402-11. doi: 10.1128/mcb.14.8.5402-5411.1994. Mol Cell Biol. 1994. PMID: 7518562 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Research Materials
Miscellaneous