钙调蛋白在组织培养细胞中的易化核转运。
Facilitated nuclear transport of calmodulin in tissue culture cells.
作者信息
Pruschy M, Ju Y, Spitz L, Carafoli E, Goldfarb D S
机构信息
Institute für Biochemie III, ETH-Zentrum, CH-8092 Zürich.
出版信息
J Cell Biol. 1994 Dec;127(6 Pt 1):1527-36. doi: 10.1083/jcb.127.6.1527.
Abstract
Calmodulin (CaM) potentiates Ca(2+)-dependent signaling pathways in both the cytoplasm and nucleus. We have investigated the mechanism of CaM nuclear transport using tissue culture cell microinjection and a permeabilized cell import assay. The inhibition of CaM import by the translocation inhibitor wheat germ agglutinin (WGA) and by chilling, indicates that CaM import is facilitated, but because ATP depletion does not affect CaM import, the mechanism does not appear to be active. Chilling and WGA arrest persist in ATP-depleted cells, indicating that CaM is not retained in the cytoplasm by an ATP-dependent mechanism. In permeabilized cells, both Ca(2+)-CaM and Ca(2+)-free CaM are sensitive to extract-dependent WGA and chilling import inhibition. Titration experiments in microinjected and permeabilized cells indicate that a saturable cytosolic factor(s) mediates chilling and WGA arrest.
摘要
钙调蛋白（CaM）可增强细胞质和细胞核中依赖钙离子的信号通路。我们利用组织培养细胞显微注射和通透细胞导入试验研究了CaM核转运的机制。易位抑制剂麦胚凝集素（WGA）和低温对CaM导入的抑制作用表明，CaM的导入是有促进作用的，但由于ATP耗竭并不影响CaM的导入，所以该机制似乎并非主动机制。在ATP耗竭的细胞中，低温和WGA阻滞作用依然存在，这表明CaM不会通过依赖ATP的机制滞留在细胞质中。在通透细胞中，钙离子-CaM和无钙CaM对依赖提取物的WGA和低温导入抑制均敏感。显微注射和通透细胞中的滴定实验表明，一种可饱和的胞质因子介导了低温和WGA阻滞作用。
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