TRANSFORMATION BY RAS ONCOGENE INDUCES NUCLEAR SHIFT OF PROTEIN-KINASE-C

被引:22
作者
CHIARUGI, V
MAGNELLI, L
PASQUALI, F
VANNUCCHI, S
BRUNI, P
QUATTRONE, A
BASI, G
CAPACCIOLI, S
RUGGIERO, M
机构
[1] Laboratory of Molecular Biology, Institute of General Pathology, University of Firenze, 50134 Firenze
关键词
D O I
10.1016/S0006-291X(05)80066-X
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
We measured protein kinase C (PKC) activity in normal and ras-transformed Balb/3T3 fibroblasts; cytosolic and nuclear-associated PKC activity was determined either as phorbol ester binding, PKC-dependent phosphorylation of histone III-S, or phosphorylation of endogenous nuclear proteins. Results demonstrate that ras-transformed fibroblasts show down-regulation of cytosolic PKC accompanied by increase of nuclear-associated PKC. These results provide evidence linking transformation to PKC nuclear shift with consequent phosphorylation of nuclear proteins. © 1990 Academic Press, Inc.
引用
收藏
页码:528 / 533
页数:6
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