Association between v-Src and protein kinase C δ in v-Src-transformed fibroblasts

Qun Zang, Zhimin Lu, Marcello Curto, Nancy Barile, David Shalloway, David A. Foster

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95 Scopus citations


In response to the kinase activity of v-Src there is an increase in the membrane association of the novel protein kinase C (PKC) isoform PKC δ (Zang, Q., Frankel, P., and Foster, D.A. (1995) Cell Growth Differ. 6, 1367- 1373). We report here that in v-Src-transformed cells PKC co- immunoprecipitates with v-Src and is phosphorylated on tyrosine. The tyrosine-phosphorylated PKC had reduced enzymatic activity relative to the non-tyrosine-phosphorylated PKC δ from v-Src-transformed cells. The association between Src and PKC δ was dependent upon both an active Src kinase and membrane association. The association between c-Src Y527F and PKC δ was substantially enhanced by mutating a PKC phosphorylation site at Ser- 12 in Src to Ala indicating that PKC δ phosphorylation of Src at Ser-12 destabilizes the interaction, possibly in a negative feedback loop. These data demonstrate that upon recruitment of PKC to the membrane in v-Src- transformed cells there is the formation of a Src·PKC δ complex in which PKC δ becomes phosphorylated on tyrosine and down-regulated.

Original languageEnglish (US)
Pages (from-to)13275-13280
Number of pages6
JournalJournal of Biological Chemistry
Issue number20
StatePublished - May 16 1997

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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