Tyrosine phosphorylation of protein kinase C-delta in response to its activation.
作者： W. Li , H. Mischak , J.C. Yu , L.M. Wang , J.F. Mushinski
DOI: 10.1016/S0021-9258(17)41948-X
关键词: Receptor tyrosine kinase 、 Phosphorylation 、 Biology 、 SH2 domain 、 Tyrosine phosphorylation 、 Protein phosphorylation 、 Tyrosine kinase 、 Molecular biology 、 Protein tyrosine phosphatase 、 Proto-oncogene tyrosine-protein kinase Src
摘要: Retroviral vectors containing five different protein kinase C (PKC) isoenzymes (alpha, delta, epsilon, eta, zeta) were expressed in 32D hematopoietic cells and NIH-3T3 fibroblasts. In an effort to investigate signaling events regulated by PKC activation, we analyzed whether tyrosine phosphorylation of cellular proteins would occur after 12-O-tetradecanoylphorbol-13-acetate (TPA) treatment the various transfectants. While no detectable tyrosine-specific was observed majority transfectants, pronounced TPA-dependent 82-kDa detected 32D/PKC-delta NIH-3T3/PKC-delta lines. Interestingly, substrate proved be PKC-delta itself. Tyrosine purified src family or receptor kinases vitro enhanced activity, suggesting that may positively affect its function.
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