Cell
Volume 49, Issue 1, 10 April 1987, Pages 65-73
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Article
Activation and suppression of pp60c-src transforming ability by mutation of its primary sites of tyrosine phosphorylation

https://doi.org/10.1016/0092-8674(87)90756-2Get rights and content

Abstract

pp60c-src is phosphorylated in vivo at tyrosine 527, a residue not present in pp60v-src (its transforming homolog), and not at tyrosine 416, its site of in vitro autophosphorylation. To test the hypothesis that tyrosine phosphorylation regulates pp60c-src biological activity, we constructed and studied pp60c-src mutants in which Tyr 527 and Tyr 416 were separately or coordinately altered to phenylalanine. Tyr→Phe 527 mutation strongly activated pp60c-src transforming and kinase activities, whereas the additional introduction of a Tyr→Phe 416 mutation suppressed these activities. Tyr→Phe 416 mutation of normal pp60c-src eliminated its partial transforming activity, which suggests that transient or otherwise restricted phosphorylation of Tyr 416 is important for pp60c-src function even though stable phosphorylation is not observed in vivo.

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