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Activation of mitogen‐activated protein kinase by protein kinase C isotypes α, β I and γ, but not ϵ
Author(s) -
Young Stephen W.,
Dickens Martin,
Tavaré Jeremy M.
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00287-6
Subject(s) - map2k7 , map kinase kinase kinase , mitogen activated protein kinase kinase , cyclin dependent kinase 9 , ask1 , cyclin dependent kinase 2 , protein kinase a , c raf , protein kinase c , microbiology and biotechnology , gene isoform , protein kinase r , chemistry , mitogen activated protein kinase , biology , kinase , biochemistry , gene
Treatment of CHO.T cells with either PMA or insulin led to the activation of MAP kinase by ∼3‐fold, and p90 rsk by ∼ 4‐fold. Over‐expression of the α, β I or γ isoforms of protein kinase C caused a substantial enhancement of the effect of PMA on the activation of MAP kinase and p90 rsk , however, the effect of insulin was unchanged. Over‐expression of the ϵ isoform of protein kinase C did not alter the effect of either PMA or insulin on the activation of MAP kinase and p90 rsk . The results suggest that protein kinase C isotypes α, β I and γ, but not ϵ, can mediate MAP kinase activation by PMA, and strongly support the hypothesis that protein kinase C isoforms can initiate distinct signalling pathways.