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pp60 c‐src is a substrate for phosphorylation when cells are stimulated to enter cycle
Author(s) -
Tamura Teruko,
Friis Robert R.,
Bauer Heinz
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)81001-7
Subject(s) - phosphoprotein , phosphorylation , proto oncogene tyrosine protein kinase src , cell cycle , chemistry , biochemistry , cell growth , microbiology and biotechnology , serine , cell , biology
The endogenous cellular oncogene products, pp60 c‐src , exhibits a protein kinase activity, but is itself a phosphoprotein. Based on the assumption that pp60 c‐src might play a role in the control of cell proliferation, we have studied its behaviour as a substrate for phosphorylation known to occur when quiescent, serum‐deprived cells are stimulated to enter cell cycle following addition of either serum, platelet‐derived growth factor or the phorbol ester derivative, 12‐ 0 ‐tetradecanoyl‐phorbol‐13‐acetate. For this purpose a partial purification of pp60 c‐src on DEAE ion‐exchange chromatography was combined with immune precipitation. A 2–4‐fold increase in serine phosphorylation of pp60 c‐src was consistently observed after stimulation of quiescent cells to growth.