Abstract
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.
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