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秀丽隐杆线虫中的紧密连接蛋白家族蛋白。

Claudin family proteins in Caenorhabditis elegans.

作者信息

Simske Jeffrey S, Hardin Jeff

出版信息

Methods Mol Biol. 2011;762:147-69. doi: 10.1007/978-1-61779-185-7_11.

DOI:10.1007/978-1-61779-185-7_11
PMID:21717355
Abstract

In the last decade, the claudin family of integral membrane proteins has been identified as the major protein component of the tight junctions in all vertebrates. The claudin superfamily proteins also function to regulate channel activity, intercellular signaling, and cell morphology. Subsequently, claudin homologues have been identified in invertebrates, including Drosophila and Caenorhabditis elegans. Recent studies demonstrate that the C. elegans claudins, clc-1 to clc-5, and similar proteins in the greater PMP22/EMP/claudin/calcium channel γ subunit family, including nsy-1-nsy-4 and vab-9, while highly divergent at a sequence level from each other and from the vertebrate claudins, in some cases play roles similar to those traditionally assigned to their vertebrate homologues. These include regulating cell adhesion and passage of small molecules through the paracellular space. The claudin superfamily proteins also function to regulate channel activity, intercellular signaling, and cell morphology. Study of claudin superfamily proteins in C. elegans should continue to provide clues as to how core claudin protein function can be modified to serve various specific roles at regions of cell-cell contact in metazoans.

摘要

在过去十年中,整合膜蛋白的claudin家族已被确定为所有脊椎动物紧密连接的主要蛋白质成分。claudin超家族蛋白还具有调节通道活性、细胞间信号传导和细胞形态的功能。随后,在包括果蝇和秀丽隐杆线虫在内的无脊椎动物中发现了claudin同源物。最近的研究表明,秀丽隐杆线虫的claudin,即clc-1至clc-5,以及更大的PMP22/EMP/claudin/钙通道γ亚基家族中的类似蛋白,包括nsy-1至nsy-4和vab-9,虽然在序列水平上彼此之间以及与脊椎动物的claudin高度不同,但在某些情况下发挥的作用类似于传统上赋予其脊椎动物同源物的作用。这些作用包括调节细胞粘附以及小分子通过细胞旁间隙的过程。claudin超家族蛋白还具有调节通道活性、细胞间信号传导和细胞形态的功能。对秀丽隐杆线虫中claudin超家族蛋白的研究应继续为后生动物细胞间接触区域中核心claudin蛋白功能如何被修饰以发挥各种特定作用提供线索。

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