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首页> 外文期刊>Molecular biology of the cell >Lens Connexins alpha 3Cx46 and alpha 8Cx50 interact with zonula occludens protein-1 (ZO-1)
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Lens Connexins alpha 3Cx46 and alpha 8Cx50 interact with zonula occludens protein-1 (ZO-1)

机译：晶状体连接蛋白alpha 3Cx46和alpha 8Cx50与闭合小带蛋白1（ZO-1）相互作用

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Connexin alpha1Cx43 has previously been shown to bind to the PDZ domain-containing protein ZO-1. The similarity of the carboxyl termini of this, connexin and the lens fiber connexins alpha3Cx46 and alpha8Cx50 suggested that these connexins may also interact with ZO-1. ZO-1 was shown to be highly expressed in mouse lenses, Colocalization of ZO-1 with alpha3Cx46 and alpha8Cx50 connexins in fiber cells was demonstrated by immunofluorescence and by fracture-labeling electron microscopy but showed regional variations throughout the lens. ZO-1 was found to coimmunoprecipitate with alpha3Cx46 and alpha8Cx50, and pull-down experiments showed that the second PDZ domain of ZO-1 was, involved in this interaction. Transiently expressed alpha3Cx46 and alpha8Cx50 connexins lacking the COOH-terminal residues did not bind to the second PDZ domain but still formed structures resembling gap junctions by immunofluorescence. These results indicate that ZO-1 interacts with lens fiber connexins alpha3Cx46 and alpha8Cx50 in a manner similar to that previously described for alpha1Cx43. The spatial variation in the interaction of ZO-1 with lens gap junctions is intriguing and is suggestive of multiple dynamic roles for this association. [References: 51]
机译：连接蛋白alpha1Cx43先前已显示与包含PDZ域的蛋白质ZO-1结合。连接蛋白和晶状体纤维连接蛋白α3Cx46和α8Cx50羧基末端的相似性表明，这些连接蛋白也可能与ZO-1相互作用。 ZO-1被证明在小鼠晶状体中高度表达，ZO-1与alpha3Cx46和alpha8Cx50连接蛋白在纤维细胞中的共定位通过免疫荧光和断裂标记电子显微镜证实，但在整个晶状体中显示出区域差异。发现ZO-1与alpha3Cx46和alpha8Cx50共免疫沉淀，下拉实验表明ZO-1的第二个PDZ结构域参与了这种相互作用。缺少COOH末端残基的瞬时表达的alpha3Cx46和alpha8Cx50连接蛋白不与第二个PDZ域结合，但仍通过免疫荧光形成类似于缺口连接的结构。这些结果表明，ZO-1与晶状体纤维连接蛋白alpha3Cx46和alpha8Cx50相互作用的方式类似于先前对alpha1Cx43所述的方式。 ZO-1与晶状体间隙连接的相互作用中的空间变化很有趣，并暗示了这种关联的多重动态作用。 [参考：51]

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