Platelet-derived growth factor induces multisite phosphorylation of pp60c-src and increases its protein-tyrosine kinase activity.

Gould KL, Hunter T
Mol Cell Biol. 1988 8 (8): 3345-56

PMID: 2463476 · PMCID: PMC363570 · DOI:10.1128/mcb.8.8.3345

We have shown previously that pp60c-src is a substrate for protein kinase C in vivo and that the target of protein kinase C phosphorylation in mammalian pp60c-src is serine 12. We now demonstrate that in addition to tumor promoters, all activators of phosphatidylinositol turnover that we have tested in fibroblasts (platelet-derived growth factor, fibroblast growth factor, serum, vasopressin, sodium orthovanadate, and prostaglandin F2 alpha) lead to the phosphorylation of pp60c-src at serine 12. In addition to stimulating serine 12 phosphorylation in pp60c-src, platelet-derived growth factor treatment of quiescent fibroblasts induces phosphorylation of one or two additional serine residues and one tyrosine residue within the N-terminal 16 kilodaltons of the enzyme and activates its immune complex protein-tyrosine kinase activity.

MeSH Terms (13)

Amino Acids Animals Cells, Cultured Kinetics Mice Peptide Mapping Phosphopeptides Phosphoproteins Phosphorylation Platelet-Derived Growth Factor Protein-Tyrosine Kinases Proto-Oncogene Proteins Proto-Oncogene Proteins pp60(c-src)

Connections (1)

This publication is referenced by other Labnodes entities:

Links