Umetsu Yoshitaka, Goda Natsuko, Taniguchi Ryo, Satomura Kaori, Ikegami Takahisa, Furuse Mikio, Hiroaki Hidekazu
Division of Structural Biology Graduate School of Medicine, Kobe University, Kobe, Hyogo, Japan.
Biomol NMR Assign. 2011 Oct;5(2):207-10. doi: 10.1007/s12104-011-9301-x. Epub 2011 Mar 24.
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 (15)N, (13)C, and (1)H 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.
闭锁小带蛋白1（ZO-1）是一种对细胞间粘附结构形成至关重要的支架分子，如紧密连接（TJ）和黏着连接（AJ）。ZO-1包含三个PDZ结构域，随后是一个GUK结构域和一个ZU5结构域。ZO-1的第一个PDZ结构域（ZO-1(PDZ1)）作为蛋白质-蛋白质相互作用模块，与几乎所有claudin蛋白的C末端相互作用，从而在侧膜上启动带状结构的形成，进而促进紧密连接的形成。最近有报道称，所有PDZ结构域中约15%能结合磷酸肌醇，ZO-1(PDZ1)就是其中之一。在此，我们报道了小鼠ZO-1第一个PDZ结构域的（15）N、（13）C和（1）H化学位移归属。本研究中获得的共振归属可能有助于阐明ZO-1(PDZ1)-claudin和ZO-1(PDZ1)-磷脂这两种二元相互作用之间的相互作用，并提示磷脂信号通路下游细胞间粘附机制形成和维持的一种新调控机制。
