A PROTEIN-KINASE-C ISOZYME IS TRANSLOCATED TO CYTOSKELETAL ELEMENTS ON ACTIVATION

被引:255
作者
MOCHLYROSEN, D
HENRICH, CJ
CHEEVER, L
KHANER, H
SIMPSON, PC
机构
[1] UNIV CALIF SAN FRANCISCO,DEPT MED,SAN FRANCISCO,CA 94143
[2] UNIV CALIF SAN FRANCISCO,CARDIOVASC RES INST,SAN FRANCISCO,CA 94143
[3] UNIV CALIF SAN FRANCISCO,DEPT PHARMACOL,SAN FRANCISCO,CA 94143
[4] SAN FRANCISCO GEN HOSP,ERNEST GALLO CLIN & RES CTR,SAN FRANCISCO,CA 94110
[5] VET ADM MED CTR,DIV CARDIOL 111-C,SAN FRANCISCO,CA 94121
[6] VET ADM MED CTR,RES SERV,SAN FRANCISCO,CA 94121
来源
CELL REGULATION | 1990年 / 1卷 / 09期
关键词
D O I
10.1091/mbc.1.9.693
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Protein kinase C (PKC)1 isozymes comprise a family of related cytosolic kinases that translocate to the cell participate fraction on stimulation. The activated enzyme is thought to be on the plasma membrane. However, phosphorylation of protein substrates occurs throughout the cell and is inconsistent with plasma membrane localization. Using an isozyme-specific monoclonal antibody we found that, on activation, this PKC isozyme translocates to myofibrils in cardiac myocytes and to microfilaments in fibroblasts. Translocation of this activated PKC isozyme to cytoskeletal elements may explain some of the effects of PKC on cell contractility and morphology. In addition, differences in the translocation site of individual isozymes - and, therefore, phosphorylation of different substrates localized at these sites - may explain the diverse biological effects of PKC. © 1990 by The American Society for Cell Biology.
引用
收藏
页码:693 / 706
页数:14
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