4K1N
Crystal structure of full-length mouse alphaE-catenin
Summary for 4K1N
| Entry DOI | 10.2210/pdb4k1n/pdb |
| Related | 4K1O |
| Descriptor | Catenin alpha-1 (1 entity in total) |
| Functional Keywords | four-helix bundle, cell adhesion, beta-catenin, f-actin |
| Biological source | Mus musculus (mouse) |
| Cellular location | Cytoplasm, cytoskeleton: P26231 |
| Total number of polymer chains | 2 |
| Total formula weight | 201624.03 |
| Authors | Ishiyama, N.,Ikura, M. (deposition date: 2013-04-05, release date: 2013-05-01, Last modification date: 2023-09-20) |
| Primary citation | 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 Cited by 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: 23589308DOI: 10.1074/jbc.M113.453928 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (6.5 Å) |
Structure validation
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