6O3E

mouse aE-catenin 82-883

6O3E の概要

• エントリーDOI: 10.2210/pdb6o3e/pdb
• 分子名称: Catenin alpha-1 (1 entity in total)
• 機能のキーワード: catenin, cell adhesion, actin binding
• 由来する生物種: Mus musculus (Mouse)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 178136.78

構造登録者

Pokutta, S.,Weis, W.I. (登録日: 2019-02-26, 公開日: 2019-11-13, 最終更新日: 2023-10-11)

主引用文献

Terekhova, K.,Pokutta, S.,Kee, Y.S.,Li, J.,Tajkhorshid, E.,Fuller, G.,Dunn, A.R.,Weis, W.I.
Binding partner- and force-promoted changes in alpha E-catenin conformation probed by native cysteine labeling.
Sci Rep, 9:15375-15375, 2019

PubMed Abstract: Adherens Junctions (AJs) are cell-cell adhesion complexes that sense and propagate mechanical forces by coupling cadherins to the actin cytoskeleton via β-catenin and the F-actin binding protein αE-catenin. When subjected to mechanical force, the cadherin•catenin complex can tightly link to F-actin through αE-catenin, and also recruits the F-actin-binding protein vinculin. In this study, labeling of native cysteines combined with mass spectrometry revealed conformational changes in αE-catenin upon binding to the E-cadherin•β-catenin complex, vinculin and F-actin. A method to apply physiologically meaningful forces in solution revealed force-induced conformational changes in αE-catenin when bound to F-actin. Comparisons of wild-type αE-catenin and a mutant with enhanced vinculin affinity using cysteine labeling and isothermal titration calorimetry provide evidence for allosteric coupling of the N-terminal β-catenin-binding and the middle (M) vinculin-binding domain of αE-catenin. Cysteine labeling also revealed possible crosstalk between the actin-binding domain and the rest of the protein. The data provide insight into how binding partners and mechanical stress can regulate the conformation of full-length αE-catenin, and identify the M domain as a key transmitter of conformational changes.

PubMed: 31653927
DOI: 10.1038/s41598-019-51816-3

実験手法

X-RAY DIFFRACTION (4.001 Å)