ACTIVATION OF YRP KINASE BY V-SRC AND PROTEIN-KINASE C-MEDIATED SIGNAL-TRANSDUCTION PATHWAYS

被引:2
作者
SCHOLZ, G
FELDER, MP
HANAFUSA, H
机构
[1] ROCKEFELLER UNIV,MOLEC ONCOL LAB,NEW YORK,NY 10021
[2] CTR UNIV ORSAY,INST CURIE,F-91405 ORSAY,FRANCE
关键词
D O I
10.1073/pnas.92.7.2592
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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 overespression 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.
引用
收藏
页码:2592 / 2596
页数:5
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