3L6X

Crystal structure of p120 catenin in complex with E-cadherin

3L6X の概要

• エントリーDOI: 10.2210/pdb3l6x/pdb
• 関連するPDBエントリー: 3L6Y
• 分子名称: Catenin delta-1, E-cadherin, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: p120, catenin, cadherin, e-cadherin, armadillo, arm, jmd, cell adhesion, complex, cell-cell adhesion, arvcf, delta-catenin, p0071, dp120, jac-1, cell membrane, membrane, nucleus, phosphoprotein, transcription, transcription regulation, wnt signaling pathway
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm . Isoform 1A: Nucleus . Isoform 2A: Nucleus . Isoform 3A: Nucleus : O60716
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 67754.18

構造登録者

Ishiyama, N.,Lee, S.-H.,Liu, S.,Li, G.-Y.,Smith, M.J.,Reichardt, L.F.,Ikura, M. (登録日: 2009-12-27, 公開日: 2010-04-21, 最終更新日: 2023-09-06)

主引用文献

Ishiyama, N.,Lee, S.H.,Liu, S.,Li, G.Y.,Smith, M.J.,Reichardt, L.F.,Ikura, M.
Dynamic and static interactions between p120 catenin and E-cadherin regulate the stability of cell-cell adhesion.
Cell(Cambridge,Mass.), 141:117-128, 2010

PubMed Abstract: The association of p120 catenin (p120) with the juxtamembrane domain (JMD) of the cadherin cytoplasmic tail is critical for the surface stability of cadherin-catenin cell-cell adhesion complexes. Here, we present the crystal structure of p120 isoform 4A in complex with the JMD core region (JMD(core)) of E-cadherin. The p120 armadillo repeat domain contains modular binding pockets that are complementary to electrostatic and hydrophobic properties of the JMD(core). Single-residue mutations within the JMD(core)-binding site of p120 abolished its interaction with E- and N-cadherins in vitro and in cultured cells. These mutations of p120 enabled us to clearly differentiate between N-cadherin-dependent and -independent steps of neuronal dendritic spine morphogenesis crucial for synapse development. NMR studies revealed that p120 regulates the stability of cadherin-mediated cell-cell adhesion by associating with the majority of the JMD, including residues implicated in clathrin-mediated endocytosis and Hakai-dependent ubiquitination of E-cadherin, through its discrete "dynamic" and "static" binding sites.

PubMed: 20371349
DOI: 10.1016/j.cell.2010.01.017

実験手法

X-RAY DIFFRACTION (2.4 Å)