4K1N

Crystal structure of full-length mouse alphaE-catenin

4K1N の概要

• エントリーDOI: 10.2210/pdb4k1n/pdb
• 関連するPDBエントリー: 4K1O
• 分子名称: Catenin alpha-1 (1 entity in total)
• 機能のキーワード: four-helix bundle, cell adhesion, beta-catenin, f-actin
• 由来する生物種: Mus musculus (mouse)
• 細胞内の位置: Cytoplasm, cytoskeleton: P26231
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 201624.03

構造登録者

Ishiyama, N.,Ikura, M. (登録日: 2013-04-05, 公開日: 2013-05-01, 最終更新日: 2023-09-20)

主引用文献

Ishiyama, N.,Tanaka, N.,Abe, K.,Yang, Y.J.,Abbas, Y.M.,Umitsu, M.,Nagar, B.,Bueler, S.A.,Rubinstein, J.L.,Takeichi, M.,Ikura, M.
An autoinhibited structure of alpha-catenin and its implications for vinculin recruitment to adherens junctions.
J.Biol.Chem., 288:15913-15925, 2013

PubMed Abstract: α-Catenin is an actin- and vinculin-binding protein that regulates cell-cell adhesion by interacting with cadherin adhesion receptors through β-catenin, but the mechanisms by which it anchors the cadherin-catenin complex to the actin cytoskeleton at adherens junctions remain unclear. Here we determined crystal structures of αE-catenin in the autoinhibited state and the actin-binding domain of αN-catenin. Together with the small-angle x-ray scattering analysis of full-length αN-catenin, we deduced an elongated multidomain assembly of monomeric α-catenin that structurally and functionally couples the vinculin- and actin-binding mechanisms. Cellular and biochemical studies of αE- and αN-catenins show that αE-catenin recruits vinculin to adherens junctions more effectively than αN-catenin, partly because of its higher affinity for actin filaments. We propose a molecular switch mechanism involving multistate conformational changes of α-catenin. This would be driven by actomyosin-generated tension to dynamically regulate the vinculin-assisted linkage between adherens junctions and the actin cytoskeleton.

PubMed: 23589308
DOI: 10.1074/jbc.M113.453928

実験手法

X-RAY DIFFRACTION (6.5 Å)