The molecular organization of tight junctions.
The molecular organization of tight junctions.
复制标题
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
中科院分区:
文献类型:
--
作者:
Citi, S
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.