The molecular organization of tight junctions.

The molecular organization of tight junctions.
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紧密连接的分子组织。

DOI:
10.1083/jcb.121.3.485
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发表时间:
1993-05
影响因子:
7.8
通讯作者:
Citi, S
Citi, S
中科院分区:
生物学1区
文献类型:
--
作者:
Citi, S

文献摘要

被引文献

相似文献

自鉴定ZO-1以来已有七年,ZO-1是第一种定位于紧密连接(TJ)t的蛋白质(60)。两年后,第二种TJ相关蛋白质,cingulin,被鉴定出来(9)。最近,两个额外的蛋白质,ZO-2(26)和7 H6(68),已被添加到列表中。根据形态学和/或生化标准,所有这些蛋白质都属于TJ的细胞质”斑块”结构域。在上皮极化细胞中,TJ(闭合小带)(综述见参考文献23、56)代表了包括粘附小带和桥粒在内的三联连接复合体的顶端成分(16)。在这一期中,Tsukitas的小组(32)报道了一种220 kD蛋白的克隆,该蛋白最初在非上皮细胞中含有钙粘蛋白的细胞-细胞接触位点的底层被鉴定(31),并将其表征为ZO-1的小鼠同源物。ZO-1/220-kD蛋白在非上皮组织中的出现(也参见参考文献29)对其作为TJ排他性标记物的特异性提出了质疑,并强调了基于其功能特性、组成和形态对连接进行分类的重要性。ZO-1/220-kD蛋白与血影蛋白的相互作用(31)及其与钙粘蛋白的共定位(31,32)提出了关于这些蛋白在TJ组装和功能中的作用的新问题。这个小的审查将讨论这些新的观点,在过去的努力和最近的进展的背景下,了解组织上皮TJs。
T is seven years since the identification of ZO-1, the first protein localized at tight junctions (TJs) t (60). Two years later, a second TJ-associated protein, cingulin, was characterized (9). More recently, two additional proteins, ZO-2 (26) and 7H6 (68), have been added to the list. All these proteins belong to the cytoplasmic" plaque" domain of TJs, based on morphological and/or biochemical criteria. In epithelial polarized cells TJs (zonulae occludentes)(for reviews see references 23, 56) represent the apical element of a tripartite junctional complex, including the zonula adhaerens and the desmosome (16). In this issue, Tsukitas's group (32) reports the cloning of a 220-kD protein, originally identified at the undercoat of cadherin-containing cell-cell contact sites, in nonepithelial cells (31) and its characterization as the mouse homologue of ZO-1. The occurrence of ZO-1/220-kD protein in nonepithelial tissues (see also reference 29) casts doubt on its specificity as a T J-exclusive marker and emphasizes the importance of classifying junctions based on their functional properties, composition and morphology. The interaction of ZO-1/220-kD protein with spectrin (31) and its colocalization with cadherins (31, 32) raises new questions about the roles of these proteins in TJ assembly and function. This mini-review will discuss these new perspectives, in the context of past efforts and recent progress in understanding the organization of epithelial TJs.