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钙黏蛋白与肌动蛋白细胞骨架的相互作用。

Interaction of cadherin with the actin cytoskeleton.

作者信息

Nelson W James, Drees Frauke, Yamada Soichiro

机构信息

Department of Molecular and Cellular Physiology, Beckman Center for Molecular and Genetic Medicine, Stanford University School of Medicine, CA 94305-5435, USA.

出版信息

Novartis Found Symp. 2005;269:159-68; discussion 168-77, 223-30.

PMID:16358407
Abstract

Cadherins regulate cell-cell adhesion throughout embryonic development and in the adult organism, and defects in cadherin expression and function are characteristic of many disease states including cancer. Although extracellular binding between cadherins specifies adhesion between cells, the strength of the interaction is thought to be regulated by cadherin clustering through reorganization of the actin cytoskeleton. Protein-protein interactions have been described that could link cadherins either directly or indirectly to the actin cytoskeleton. Here, we describe these protein interactions, and examine critically the evidence that they link cadherins to the actin cytoskeleton.

摘要

钙黏蛋白在整个胚胎发育过程以及成体生物体中调节细胞间黏附,钙黏蛋白表达和功能的缺陷是包括癌症在内的许多疾病状态的特征。虽然钙黏蛋白之间的细胞外结合决定了细胞间的黏附,但这种相互作用的强度被认为是通过肌动蛋白细胞骨架的重组使钙黏蛋白聚集来调节的。已经描述了一些蛋白质 - 蛋白质相互作用,它们可以直接或间接地将钙黏蛋白与肌动蛋白细胞骨架联系起来。在这里,我们描述这些蛋白质相互作用,并严格审查它们将钙黏蛋白与肌动蛋白细胞骨架联系起来的证据。

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Cingulin and paracingulin show similar dynamic behaviour, but are recruited independently to junctions.cingulin和副cingulin表现出相似的动态行为,但它们是独立招募到连接处的。
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Endocytosis of cadherin from intracellular junctions is the driving force for cadherin adhesive dimer disassembly.来自细胞内连接的钙黏蛋白内吞作用是钙黏蛋白黏附二聚体解离的驱动力。
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