A PROTEIN-KINASE-C ISOZYME IS TRANSLOCATED TO CYTOSKELETAL ELEMENTS ON ACTIVATION
A PROTEIN-KINASE-C ISOZYME IS TRANSLOCATED TO CYTOSKELETAL ELEMENTS ON ACTIVATION
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DOI：
10.1091/mbc.1.9.693
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发表时间：
1990-08-01
期刊：
影响因子：
--
通讯作者：
SIMPSON, PC
中科院分区：
文献类型：
--
作者：
MOCHLYROSEN, D;HENRICH, CJ;SIMPSON, PC
蛋白激酶C(PKC)1同工酶包括一组相关的胞浆蛋白激酶，它们在刺激时转移到细胞颗粒部分。被激活的酶被认为是在质膜上。然而，蛋白质底物的磷酸化发生在整个细胞中，与质膜定位不一致。使用同工酶特异性的单抗，我们发现，在激活时，这种PKC同工酶转位到心肌细胞中的肌原纤维和成纤维细胞中的微丝。这种被激活的PKC同工酶转移到细胞骨架元件上可能解释了PKC对细胞收缩和形态的一些影响。此外，个别同工酶易位部位的差异--以及这些部位不同底物的磷酸化--可能解释了PKC的不同生物学效应。
Protein kinase C (PKC)1 isozymes comprise a family of related cytosolic kinases that translocate to the cell particulate 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.