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. 1988 Oct;8(10):4541-6.
doi: 10.1128/mcb.8.10.4541-4546.1988.

Regulation by the autophosphorylation site in overexpressed pp60c-src

T E Kmiecik  1 , P J Johnson, D Shalloway
Affiliations

Regulation by the autophosphorylation site in overexpressed pp60c-src

T E Kmiecik et al. Mol Cell Biol. 1988 Oct.

Abstract

We show that overexpressed pp60c-src is phosphorylated at Tyr-416 and has increased specific kinase activity when isolated from cells incubated with vanadate, a tyrosine phosphatase inhibitor. This supports the hypothesis that transient Tyr-416 phosphorylation modulates the activity of overexpressed pp60c-src in vivo. Mutagenesis indicates that Tyr-416 modulates pp60v-src activity as well.

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