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. 1988 Oct;8(10):4541–4546. doi: 10.1128/mcb.8.10.4541

Regulation by the autophosphorylation site in overexpressed pp60c-src.

T E Kmiecik 1, P J Johnson 1, D Shalloway 1
PMCID: PMC365532  PMID: 2460746

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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Selected References

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