title: 1H, 13C, and 15N resonance assignment of the first PDZ domain of mouse ZO-1.
abstract: 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.
authors: Division of Structural Biology Graduate School of Medicine, Kobe University, Kobe, Hyogo, Japan.
authors: Yoshitaka
authors: Y
authors: Umetsu
authors: Natsuko
authors: N
authors: Goda
authors: Ryo
authors: R
authors: Taniguchi
authors: Kaori
authors: K
authors: Satomura
authors: Takahisa
authors: T
authors: Ikegami
authors: Mikio
authors: M
authors: Furuse
authors: Hidekazu
authors: H
authors: Hiroaki
mesh_terms: D000818:Animals; D007554:Isotopes; D008565:Membrane Proteins / Q000737:chemistry*; D051379:Mice; D019906:Nuclear Magnetic Resonance, Biomolecular; D054731:PDZ Domains; D010750:Phosphoproteins / Q000737:chemistry*; D019108:Tight Junctions; D062826:Zonula Occludens-1 Protein
chemical_list: D007554:Isotopes; D008565:Membrane Proteins; D010750:Phosphoproteins; C569043:Tjp1 protein, mouse; D062826:Zonula Occludens-1 Protein