Identification of a novel protein, LYRIC, localized to tight junctions of polarized epithelial cells
Identification of a novel protein, LYRIC, localized to tight junctions of polarized epithelial cells
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DOI：
10.1016/j.yexcr.2004.06.026
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发表时间：
2004-10-15
影响因子：
3.7
通讯作者：
Hixson, DC
中科院分区：
文献类型：
--
作者：
Britt, DE;Yang, DF;Hixson, DC
紧密连接（TJ）是一种多蛋白复合物，其功能是调节分子通过上皮和内皮细胞层的细胞旁运输。近年来发现了许多新的紧密连接相关蛋白，它们的功能作用和相互作用才刚刚开始被阐明。在本文中，我们描述了一种新的富含赖氨酸的CEACAM1共分离蛋白（LYRIC），该蛋白在物种间广泛表达且高度保守。LYRIC没有表明功能的保守结构域，似乎也不是一个更大的蛋白质家族的成员。来自大鼠和人类组织切片和细胞系的分析数据表明，LYRIC在极化上皮细胞中与紧密连接蛋白ZO-1和occludin共定位，表明LYRIC是紧密连接复合物的一部分。当连接复合物被破坏时，LYRIC与ZO-1分离，当紧密连接重组时，ZO-1在LYRIC之前重新定位。这些结果表明，LYRIC很可能不是TJ形成所需的结构成分，而是在紧密连接复合物成熟过程中招募的。(C) 2004爱思唯尔公司版权所有。
Tight junctions (TJ) are multiprotein complexes that function to regulate paracellular transport of molecules through epithelial and endothelial cell layers. Many new tight junction-associated proteins have been identified in the past few years, and their functional roles and interactions have just begun to be elucidated. In this paper, we describe a novel protein LYsine-RIch CEACAM1 co-isolated (LYRIC) that is widely expressed and highly conserved between species. LYRIC has no conserved domains that would indicate function and does not appear to be a member of a larger protein family. Data from analysis of rat and human tissue sections and cell lines show that LYRIC colocalizes with tight junction proteins ZO-1 and occludin in polarized epithelial cells, suggesting that LYRIC is part of the tight junction complex. LYRIC dissociates from ZO-1 when junctional complexes are disrupted, and as tight junctions reform, ZO-1 relocalizes before LYRIC. These results suggest that LYRIC is most likely not a structural component required for TJ formation, but rather is recruited during the maturation of the tight junction complex. (C) 2004 Elsevier Inc. All rights reserved.