Open AccessNovel serine phosphorylation of pp60c-src in intact cells after tumor promoter treatment.
Author(s) -
L E Gentry,
K Chaffin,
Mohammed Shoyab,
Anthony F. Purchio
Publication year - 1986
Publication title -
molecular and cellular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.14
H-Index - 327
eISSN - 1067-8824
pISSN - 0270-7306
DOI - 10.1128/mcb.6.2.735
Subject(s) - phosphorylation , serine , biology , microbiology and biotechnology , threonine , phosphopeptide , serine protease , phosphoserine , biochemistry , tumor promotion , residue (chemistry) , proteases , protease , gene , enzyme , carcinogenesis
Treatment of normal cells with the tumor promoters 12-O-tetradecanoylphorbol-13-acetate and mezerein results in increased phosphorylation of pp60c-src. Two-dimensional tryptic phosphopeptide analysis of partial V8 protease fragments indicated that this phosphorylation takes place on a serine residue which lies within the amino-terminal 18 kilodaltons of pp60c-src and represents the major phosphorylation site following tumor promoter treatment. Untreated cells exhibited a low but detectable level of phosphorylation at this serine residue. The significance of these results with respect to the phosphoregulation of pp60c-src as well as tumor promotion is discussed.