Zinc‐induced tyrosine phosphorylation of hippocampal p6Oc‐scr is catalyzed by another protein tyrosine kinase

FEBS Letters

Loeb, Jacques¹  Vener, Alexander V.¹ 

[1] ISERM U29, 123 Boulevard de Part Royal, 75014 Paris, France

关键词: Zinc;    Protein phosphorylation;    Phosphotyrosine;    p60c-scr;    Rat hippocampus;   

DOI  :  10.1016/0014-5793(92)81058-T

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Tyrosine phosphorylation of p60^c-src induced by Zn²⁺ in rat hippocampal membranes is shown to inhibit Src tyrosine kinase activity, Zn²⁺ 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 Zn²⁺-induced activity in phosphorylation of exogenous substrate, enolase. Cyanogen bromide cleavage of p60^c-src phosphorylated in the presence of Zn²⁺ yields a 4-kDa phosphopeptide corresponding to phosphorylation of a carboxy-terminal tyrosine residue of Src kinase. In conclusion, hippocampal membranes contain a Zn²⁺-stimulated protein tyrosine kinase capable of regulating the p60^c-src activity.

【 授权许可】

Unknown