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. 1986 Feb;6(2):735–738. doi: 10.1128/mcb.6.2.735

Novel serine phosphorylation of pp60c-src in intact cells after tumor promoter treatment.

L E Gentry, K E Chaffin, M Shoyab, A F Purchio
PMCID: PMC367568  PMID: 2431272

Abstract

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.

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Selected References

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