RT Journal Article
SR Electronic
T1 PDGF alpha-receptor mediated cellular responses are not dependent on Src family kinases in endothelial cells
JF Journal of Cell Science
JO J. Cell Sci.
FD The Company of Biologists Ltd
SP 607
OP 614
VO 111
IS 5
A1 Hooshmand-Rad, R.
A1 Yokote, K.
A1 Heldin, C.H.
A1 Claesson-Welsh, L.
YR 1998
UL http://jcs.biologists.org/content/111/5/607.abstract
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.