This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
4k1n
From Proteopedia
Contents |
Crystal structure of full-length mouse alphaE-catenin
Template:ABSTRACT PUBMED 23589308
Function
[CTNA1_MOUSE] Associates with the cytoplasmic domain of a variety of cadherins. The association of catenins to cadherins produces a complex which is linked to the actin filament network, and which seems to be of primary importance for cadherins cell-adhesion properties. Can associate with both E- and N-cadherins. Originally believed to be a stable component of E-cadherin/catenin adhesion complexes and to mediate the linkage of cadherins to the actin cytoskeleton at adherens junctions. In contrast, cortical actin was found to be much more dynamic than E-cadherin/catenin complexes and CTNNA1 was shown not to bind to F-actin when assembled in the complex suggesting a different linkage between actin and adherens junctions components. The homodimeric form may regulate actin filament assembly and inhibit actin branching by competing with the Arp2/3 complex for binding to actin filaments. May play a crucial role in cell differentiation.[1]
About this Structure
4k1n is a 2 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
- Ishiyama N, Tanaka N, Abe K, Yang YJ, Abbas YM, Umitsu M, Nagar B, Bueler SA, Rubinstein JL, Takeichi M, Ikura M. An Autoinhibited Structure of alpha-catenin and Its Implications for Vinculin Recruitment to Adherens Junctions. J Biol Chem. 2013 Apr 15. PMID:23589308 doi:10.1074/jbc.M113.453928
- ↑ Drees F, Pokutta S, Yamada S, Nelson WJ, Weis WI. Alpha-catenin is a molecular switch that binds E-cadherin-beta-catenin and regulates actin-filament assembly. Cell. 2005 Dec 2;123(5):903-15. PMID:16325583 doi:10.1016/j.cell.2005.09.021
