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Regulation by the autophosphorylation site in overexpressed pp60c-src.
Authors:T E Kmiecik   P J Johnson     D Shalloway
Affiliation:Department of Molecular and Cell Biology, Pennsylvania State University, University Park, 16802.
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.
Keywords:
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