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Protein kinase C phosphorylates pp60src at a novel site.

Abstract：

: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.

journal_name

Cell

journal_title

Cell

authors

Gould KL,Woodgett JR,Cooper JA,Buss JE,Shalloway D,Hunter T

doi

10.1016/0092-8674(85)90281-8

subject

Has Abstract

pub_date

1985-10-01 00:00:00

pages

849-57

issue

3

eissn

0092-8674

issn

1097-4172

pii

0092-8674(85)90281-8

journal_volume

42

pub_type

杂志文章

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