4K1N: Crystal structure of full-length mouse alphaE-catenin

alpha-Catenin is an actin- and vinculin-binding protein that regulates cell-cell adhesion by interacting with cadherin adhesion receptors through beta-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 alphaE-catenin in the autoinhibited state and the actin-binding domain of alphaN-catenin. Together with the small-angle x-ray scattering analysis of full-length alphaN-catenin, we deduced an elongated multidomain assembly of monomeric alpha-catenin that structurally and functionally couples the vinculin- and actin-binding mechanisms. Cellular and biochemical studies of alphaE- and alphaN-catenins show that alphaE-catenin recruits vinculin to adherens junctions more effectively than alphaN-catenin, partly because of its higher affinity for actin filaments. We propose a molecular switch mechanism involving multistate conformational changes of alpha-catenin. This would be driven by actomyosin-generated tension to dynamically regulate the vinculin-assisted linkage between adherens junctions and the actin cytoskeleton.
PDB ID: 4K1NDownload
MMDB ID: 109742
PDB Deposition Date: 2013/4/5
Updated in MMDB: 2017/11
Experimental Method:
x-ray diffraction
Resolution: 6.5  Å
Source Organism:
Similar Structures:
Biological Unit for 4K1N: dimeric; determined by author and by software (PISA)
Molecular Components in 4K1N
Label Count Molecule
Proteins (2 molecules)
Catenin Alpha-1(Gene symbol: Ctnna1)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB