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首页> 外文期刊>Cell motility and the cytoskeleton >Interaction of the beta(IV)-tubulin isotype with actin stress fibers in cultured rat kidney mesangial cells.
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Interaction of the beta(IV)-tubulin isotype with actin stress fibers in cultured rat kidney mesangial cells.

机译：β（IV）-微管蛋白同种型与肌动蛋白应激纤维在培养的大鼠肾系膜细胞中的相互作用。

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摘要

Microtubules and actin filaments are two of the major components of the cytoskeleton. There is accumulating evidence for interaction between the two networks. Both the alpha- and beta-subunits of tubulin exist as numerous isotypes, some of which have been highly conserved in evolution. In an effort to better understand the functional significance of tubulin isotypes, we used a double immunofluorescence labeling technique to investigate the interactions between the tubulin beta-isotypes and the actin stress fiber network in cultured rat kidney mesangial cells, smooth-muscle-like cells from the renal glomerulus. Removal of the soluble cytoplasmic and nucleoplasmic proteins by detergent extraction caused the microtubule network to disappear while the stress fiber network was still present. In these extracted cells, the beta(I)- and beta(II)-tubulin isotypes were no longer present in the cytoplasm while the beta(IV)-isotype co-localized with actin stress fibers. Co-localization between beta(IV)-tubulin and actin stress fibers was also observed when the microtubule network was disrupted by the anti-tubulin drug colchicine and also by microinjection of the beta(IV)-tubulin antibody. Our results suggest that the beta(IV) isotype of tubulin may be involved in interactions between microtubules and actin. Copyright 2001 Wiley-Liss, Inc.
机译：微管和肌动蛋白丝是细胞骨架的两个主要组成部分。越来越多的证据表明这两个网络之间存在相互作用。微管蛋白的α亚基和β亚基都以许多同种型存在，其中一些在进化中高度保守。为了更好地了解微管蛋白同种型的功能意义，我们使用了双重免疫荧光标记技术来研究培养的大鼠肾小球系膜细胞，平滑肌样细胞中微管蛋白β同种型与肌动蛋白应激纤维网络之间的相互作用。肾小球。通过去污剂提取去除可溶性细胞质和核质蛋白会导致微管网络消失，而应力纤维网络仍然存在。在这些提取的细胞中，β（I）-和β（II）-微管蛋白同种型不再存在于细胞质中，而β（IV）-同种型与肌动蛋白应激纤维共定位。当微管网络被抗微管蛋白药物秋水仙碱以及微注射β（IV）-微管蛋白抗体破坏时，也观察到了β（IV）-微管蛋白和肌动蛋白应激纤维之间的共定位。我们的结果表明，微管蛋白的β（IV）同型可能与微管和肌动蛋白之间的相互作用有关。版权所有2001 Wiley-Liss，Inc.

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