PT  - JOURNAL ARTICLE
AU  - Hooshmand-Rad, R.
AU  - Yokote, K.
AU  - Heldin, C.H.
AU  - Claesson-Welsh, L.
TI  - PDGF alpha-receptor mediated cellular responses are not dependent on Src family kinases in endothelial cells
DP  - 1998 Mar 01
TA  - Journal of Cell Science
PG  - 607--614
VI  - 111
IP  - 5
4099  - http://jcs.biologists.org/content/111/5/607.short
4100  - http://jcs.biologists.org/content/111/5/607.full
SO  - J. Cell Sci.1998 Mar 01; 111
AB  - Two novel autophosphorylation sites in the juxtamembrane region of the PDGF alpha-receptor, Tyr-572 and Tyr-574, were identified. A Y572/574F mutant PDGF (alpha)-receptor was generated and stably expressed in porcine aortic endothelial cells. In contrast to the wild-type receptor, the mutant receptor was unable to associate with or activate Src family tyrosine kinases. Tyrosine phosphorylated synthetic peptides representing the juxtamembrane sequence of the receptor dose-dependently inhibited the binding of Src family tyrosine kinases to the autophosphorylated PDGF alpha-receptor. The mutant receptor showed similar PDGF-induced kinase activity and ability to mediate mitogenicity, actin reorganization and chemotaxis as the wild-type receptor. Thus activation of Src family kinases by the PDGF alpha-receptor is not essential for PDGF-induced mitogenicity or actin reorganization.