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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Interaction between connexin35 and zonula occludens-1 and its potential role in the regulation of electrical synapses
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Interaction between connexin35 and zonula occludens-1 and its potential role in the regulation of electrical synapses

机译：连接蛋白35和小带闭合蛋白1之间的相互作用及其在电突触调控中的潜在作用

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摘要

Although regulation of chemical transmission is known to involve the interaction of receptors with scaffold proteins, little is known about the existence of protein-protein interactions in regulating gap junction-mediated electrical synapses. The scaffold protein zonula-occludens-1 (ZO-1), a member of the MAGUK family of proteins, was reported to interact with several connexins (Cxs). We show here that ZO-1 extensively colocalizes with Cx35 at identifiable "mixed" (electrical and chemical) contacts on goldfish Mauthner cells, a model synapse for the study of vertebrate electrical transmission where it is possible to correlate physiological properties with molecular composition. Further, our analysis indicates that these proteins directly interact at goldfish electrical synapses. In contrast to Cx43, which interacts with ZO-1 via the PDZ2 domain, Cx35 interacts with ZO-1 via the PDZ1 domain, and this association is of lower affinity. The properties of the ZO-1/Cx35 association suggest the existence of a more dynamic relation between these two proteins, possibly including a role of ZO-1 in regulating gap junctional conductance at these highly modifiable electrical synapses. The interaction of ZO-1 with conserved regions of the C termini of Cx35/Cx36 orthologs may have a common function at electrical synapses of mammals and other vertebrates.
机译：尽管已知化学传递的调节涉及受体与支架蛋白的相互作用，但对于调节间隙连接介导的电突触中蛋白-蛋白相互作用的存在知之甚少。据报道，支架蛋白zonula-occludens-1（ZO-1）是MAGUK蛋白家族的成员，与几种连接蛋白（Cxs）相互作用。我们在这里显示ZO-1在金鱼Mauthner细胞上可识别的“混合”（电和化学）接触点上与Cx35广泛共定位，这是研究脊椎动物电传递的模型突触，在那里可以将生理特性与分子组成相关联。此外，我们的分析表明这些蛋白质在金鱼的电气突触中直接相互作用。与Cx43通过PDZ2域与ZO-1相互作用相反，Cx35通过PDZ1域与ZO-1相互作用，并且这种关联的亲和力较低。 ZO-1 / Cx35关联的性质表明这两个蛋白之间存在更动态的关系，可能包括ZO-1在调节这些高度可修饰的电突触中的间隙连接电导中的作用。 ZO-1与Cx35 / Cx36直系同源物C末端保守区域的相互作用可能在哺乳动物和其他脊椎动物的电突触中具有共同的功能。

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