Figure 1: Domain map and experimental setup.
From: Force-dependent conformational switch of α-catenin controls vinculin binding
(a) Domain mapping of full-length and sub-domains of mouse αE-catenin. αE-catenin consists of an N-terminal dimerization domain (DD), followed by vinculin-binding domain (VBD; also referred to the MI domain). Interaction between VBD and two other modulation domains (MII-MIII) is suggested to inhibit vinculin binding. αE-catenin contains a C-terminal F-actin-binding domain (FABD) that binds to F-actin and transmits mechanical forces generated by actomyosin contraction. The αCM construct (residues 275–735) is enclosed in the top bracket. (b) Schematics of experimental setup. A single αCM molecule is tethered between a cover glass surface and a paramagnetic bead through NTA-His tag and streptavidin-biotin linkages, respectively. The modulatory MI (VBD) domain is shown in green, MII and MIII domains in yellow. The vinculin-binding helix is marked in red. The VD1 molecule, which is also a helix bundle, is shown in silver. Force was applied to the paramagnetic bead using a pair of permanent magnets. αCM constructs were stretched in the absence or in the presence of VD1 of various concentrations. The model of αCM is adopted from PDB structure 4IGG.
