Zinc causes tyrosine phosphorylation of hippocampal p60c‐src

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Abstract
Zinc cations at concentrations of 0.2 mM and greater catalyzed specific phosphorylation, by ATP, of two membrane‐associated proteins from rat hippocampus. These proteins, corresponding to molecular weights or 60 and 49 kDa, were phosphorylated primarily at tyrosine residues. The 60‐kDa protein was identified as p60c‐src by immunoprecipitation using two different p60c‐src‐specific monoclonal antibodies. The 49‐kDa protein co‐immunoprecipitated with p60c‐src. Cyanogen bromide cleavage of p60c‐src and the 49‐kDa protein phosphorylated in the presence of Zn2+ gave different patterns or phosphopeptides. It is suggested that tyrosine phosphorylation of p60c‐src and the p60c‐src‐associated 49‐kDa protein may be a way of zinc participation in hippocampal neurotransmission.