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

L E Gentry | Zendy; Karen E. Chaffin | Zendy; M. Shoyab | Zendy; A F Purchio | Zendy

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

Author(s) -

L E Gentry,

Karen E. Chaffin,

M. Shoyab,

A 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.

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