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E-钙黏蛋白是黏着连接复合体的核心成分,它可改变果蝇间隙连接蛋白Innexin2的亚细胞定位。

DE-cadherin, a core component of the adherens junction complex modifies subcellular localization of the Drosophila gap junction protein innexin2.

作者信息

Bauer R, Weimbs A, Lechner H, Hoch M

机构信息

Institute of Molecular Physiology and Developmental Biology, University of Bonn, Bonn, Germany.

出版信息

Cell Commun Adhes. 2006 Jan-Apr;13(1-2):103-14. doi: 10.1080/15419060600631839.

Abstract

The Drosophila innexin multigene family of gap junction encoding proteins consists of eight family members whose function in epithelial morphogenesis is mostly unknown. We have recently shown that innexin2 plays a crucial role in the organization of embryonic epithelia. Innexin2 protein accumulates in the epidermis in the apico-lateral membrane domain and colocalizes with core proteins of adherens junctions, such as DE-cadherin and Armadillo, the ss -catenin homolog. Innexin2 localization is altered in both armadillo and DE-cadherin mutants Biochemical interaction studies point to a direct interaction of DE-cadherin and Armadillo with innexin2 suggesting a close link between gap junction and adherens junction biogenesis. We have used the Drosophila Schneider cell tissue culture system to further study the interaction of innexin2 with DE-cadherin. Our results provide evidence that DE-cadherin may be a key component to control trafficking, and localization of Innexin2 to the plasma membrane.

摘要

果蝇中编码间隙连接蛋白的Innexin多基因家族由八个家族成员组成,其在上皮形态发生中的功能大多未知。我们最近发现Innexin2在胚胎上皮组织的形成中起关键作用。Innexin2蛋白在表皮的顶侧膜结构域积累,并与黏着连接的核心蛋白共定位,如DE-钙黏蛋白和犰狳蛋白(β-连环蛋白的同源物)。在犰狳蛋白和DE-钙黏蛋白突变体中,Innexin2的定位发生改变。生化相互作用研究表明,DE-钙黏蛋白和犰狳蛋白与Innexin2直接相互作用,这表明间隙连接和黏着连接的生物发生之间存在密切联系。我们利用果蝇Schneider细胞组织培养系统进一步研究Innexin2与DE-钙黏蛋白的相互作用。我们的结果提供了证据,表明DE-钙黏蛋白可能是控制Innexin2运输以及其在质膜上定位的关键成分。

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