Protein kinase C phosphorylates pp60src at a novel site.

Gould KL, Woodgett JR, Cooper JA, Buss JE, Shalloway D, Hunter T
Cell. 1985 42 (3): 849-57

PMID: 2996780 · DOI:10.1016/0092-8674(85)90281-8

The transforming protein of Rous sarcoma virus (pp60v-src) and its normal cellular homolog (pp60c-src) are demonstrated to be phosphorylated at serine 12 in vivo under certain conditions. We propose that protein kinase C is responsible for this modification based on the following evidence. First, the tumor promoters, 12-O-tetradecanoylphorbol-13-acetate and teleocidin, and synthetic diacylglycerol, known activators of protein kinase C in vivo, cause nearly complete phosphorylation of pp60src at serine 12. Second, among five purified serine/threonine-specific protein kinases tested, only protein kinase C phosphorylates pp60c-src and pp60v-src in vitro at serine 12. Third, purified protein kinase C phosphorylates a synthetic peptide corresponding to the N-terminal 20 amino acids of pp60c-src at serine 12. The physiological significance of this novel phosphorylation is discussed.

MeSH Terms (18)

Amino Acid Sequence Animals Avian Sarcoma Viruses Brain Cells, Cultured Kinetics Mice Muscles Oncogene Protein pp60(v-src) Phosphorylation Protein Kinase C Protein Kinases Rabbits Rats Retroviridae Proteins Serine Substrate Specificity Tetradecanoylphorbol Acetate

Connections (1)

This publication is referenced by other Labnodes entities: