TY - JOUR
T1 - Association between v-Src and protein kinase C δ in v-Src-transformed fibroblasts
AU - Zang, Qun
AU - Lu, Zhimin
AU - Curto, Marcello
AU - Barile, Nancy
AU - Shalloway, David
AU - Foster, David A.
PY - 1997/5/16
Y1 - 1997/5/16
N2 - 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.
AB - 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.
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U2 - 10.1074/jbc.272.20.13275
DO - 10.1074/jbc.272.20.13275
M3 - Article
C2 - 9148947
AN - SCOPUS:0030976892
SN - 0021-9258
VL - 272
SP - 13275
EP - 13280
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 20
ER -