1H, 13C, and 15N resonance assignment of the first PDZ domain of mouse ZO-1
1H, 13C, and 15N resonance assignment of the first PDZ domain of mouse ZO-1
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DOI：
10.1007/s12104-011-9301-x
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发表时间：
2011-10-01
影响因子：
0.9
通讯作者：
Hiroaki, Hidekazu
中科院分区：
文献类型：
--
作者：
Umetsu, Yoshitaka;Goda, Natsuko;Hiroaki, Hidekazu
闭锁小带-1(ZO-1)是细胞间黏附结构形成的重要支架分子，如紧密连接(TJ)和黏附连接(AJ)。ZO-1包含三个PDZ结构域，后跟一个GUK结构域和一个ZU5结构域。ZO-1的第一个PDZ(ZO-1(PDZ1))作为蛋白质-蛋白质相互作用模块，与几乎所有Claudins的C末端相互作用，启动侧膜上带状结构的形成，从而促进TJ的形成。最近报道，大约15%的PDZ结构域与磷脂酰肌醇结合，ZO-1(PDZ1)就是其中之一。在这里，我们报告了小鼠ZO-1的第一个PDZ结构域的N-15，C-13和H-1化学位移指定。这项工作中获得的共振归属可能有助于阐明ZO-1(PDZ1)-claudins和ZO-1(PDZ1)-磷脂这两个二元相互作用之间的相互作用，并提出一种新的调控机制，支持磷脂信号通路下游细胞-细胞黏附机制的形成和维持。
Zonula occludens-1 (ZO-1) is a scaffolding molecule critical to the formation of intercellular adhesion structures, such as tight junctions (TJs) and adherens junctions (AJs). ZO-1 contains three PDZ domains followed by a GUK domain and a ZU5 domain. The first PDZ of ZO-1 (ZO-1(PDZ1)) serves as a protein-protein interaction module and interacts with the C-termini of almost all claudins to initiate the formation of a belt-like structure on the lateral membranes, thereby promoting TJ formation. It has been recently reported that approximately 15% of all PDZ domains bind phosphoinositides, and ZO-1(PDZ1) is the one of these. Here we report the N-15, C-13, and H-1 chemical shift assignments of the first PDZ domain of mouse ZO-1. The resonance assignments obtained in this work may contribute in clarifying the interplay between the two binary interactions, ZO-1(PDZ1)-claudins and ZO-1(PDZ1)-phospholipids, and suggesting a novel regulation mechanism underlying the formation and maintenance of cell-cell adhesion machinery downstream of the phospholipid signaling pathways.