Open AccessActivation of YRP kinase by v-Src and protein kinase C-mediated signal transduction pathways.
Author(s) -
Glen M. Scholz,
Marie-Paule Felder,
Hidesaburô Hanafusa
Publication year - 1995
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.92.7.2592
Subject(s) - cyclin dependent kinase 9 , map kinase kinase kinase , map2k7 , ask1 , mitogen activated protein kinase kinase , cyclin dependent kinase 2 , proto oncogene tyrosine protein kinase src , c raf , cyclin dependent kinase 4 , tyrosine kinase , microbiology and biotechnology , chemistry , biology , signal transduction , protein kinase a , protein kinase c , kinase
We have previously reported that a serine(threonine) protein kinase that phosphorylates histone H1 in vitro is activated by tyrosine phosphorylation in v-Src-transformed rat 3Y1 fibroblasts. We now refer to this kinase as YRP kinase, for tyrosine-regulated protein kinase. Since YRP kinase may play a role in mediating the growth-stimulatory and morphology-altering effects of v-Src, we have further examined the signal transduction involved in the activation of YRP kinase. Although YRP kinase is constitutively activated in fibroblasts transformed by v-Src, activation of protein kinase C was also found to lead to activation of YRP kinase. Activation of YRP kinase by protein kinase C was found to be potentiated by vanadate treatment or overexpression of c-Src. The activation of YRP kinase by v-Src, however, does not appear to be mediated by protein kinase C, suggesting that YRP kinase can be activated by two separate signal transduction pathways. Transformation of fibroblasts by v-Ras or v-Mil did not result in activation of YRP kinase, indicating that the MAP kinase pathway does not mediate the activation of YRP kinase by v-Src or protein kinase C.