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Zinc‐induced tyrosine phosphorylation of hippocampal p6O c‐scr is catalyzed by another protein tyrosine kinase
Author(s) -
Vener Alexander V.,
Loeb Jacques
Publication year - 1992
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(92)81058-t
Subject(s) - autophosphorylation , proto oncogene tyrosine protein kinase src , phosphorylation , tyrosine phosphorylation , chemistry , tyrosine , sh2 domain , biochemistry , tyrosine kinase , protein tyrosine phosphatase , receptor tyrosine kinase , protein phosphorylation , microbiology and biotechnology , protein kinase a , biology , signal transduction
Tyrosine phosphorylation of p60 c‐src induced by Zn 2+ in rat hippocampal membranes is shown to inhibit Src tyrosine kinase activity, Zn 2+ catalyzes the phosphorylation of p60 c‐scr in the membranes but does not activate autophosphorylation of p60 c‐scr immunoprecipitated with anti‐ Scr monoclonal antibody. Moreover, the immunoprecipitated Src kinase has no Zn 2+ ‐induced activity in phosphorylation of exogenous substrate, enolase. Cyanogen bromide cleavage of p60 c‐src phosphorylated in the presence of Zn 2+ yields a 4‐kDa phosphopeptide corresponding to phosphorylation of a carboxy‐terminal tyrosine residue of Src kinase. In conclusion, hippocampal membranes contain a Zn 2+ ‐stimulated protein tyrosine kinase capable of regulating the p60 c‐src activity.