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Science 3 March 1989:
Vol. 243. no. 4895, pp. 1191 - 1194
DOI: 10.1126/science.2466336
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Articles

Science, Vol 243, Issue 4895, 1191-1194
Copyright © 1989 by American Association for the Advancement of Science

articles

Role of phosphatidylinositol kinase in PDGF receptor signal transduction

Coughlin SR, JA Escobedo, and LT Williams

Howard Hughes Medical Institute, University of California, San Francisco 94143.

The molecules with which the platelet-derived growth factor (PDGF) receptor interacts to elicit the biochemical reactions responsible for cell proliferation have not been identified. Antisera directed against specific PDGF receptor peptides coprecipitated a phosphatidylinositol (PI) kinase and the PDGF receptor. Immunoprecipitates from PDGF-stimulated cells contained 10 to 50 times as much PI kinase as those from unstimulated cells. Mutation of the PDGF receptor by deletion of its kinase insert region resulted in a receptor markedly less effective than the wild type in eliciting cell proliferation and defective in PDGF-stimulated PI kinase, but still capable of PDGF-induced receptor autophosphorylation and phosphoinositide hydrolysis. These data show that the PDGF receptor is physically associated with a PDGF-sensitive PI kinase that is distinct from tyrosine kinase and is not required for PDGF-induced PI hydrolysis. The finding that the mutant PDGF receptor missing the kinase insert domain elicited known early biochemical responses to PDGF, but did not associate with or regulate PI kinase, suggests a novel role for the receptor-associated PI kinase in the transmission of mitogenic signals.


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