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© Research
Publication : Molecular biology of the cell

αE-catenin actin-binding domain alters actin filament conformation and regulates binding of nucleation and disassembly factors.

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Molecular biology of the cell - 01 Dec 2013

Hansen SD, Kwiatkowski AV, Ouyang CY, Liu H, Pokutta S, Watkins SC, Volkmann N, Hanein D, Weis WI, Mullins RD, Nelson WJ,

Link to Pubmed [PMID] – 24068324

Link to DOI – 10.1091/mbc.E13-07-0388

Mol Biol Cell 2013 Dec; 24(23): 3710-20

The actin-binding protein αE-catenin may contribute to transitions between cell migration and cell-cell adhesion that depend on remodeling the actin cytoskeleton, but the underlying mechanisms are unknown. We show that the αE-catenin actin-binding domain (ABD) binds cooperatively to individual actin filaments and that binding is accompanied by a conformational change in the actin protomer that affects filament structure. αE-catenin ABD binding limits barbed-end growth, especially in actin filament bundles. αE-catenin ABD inhibits actin filament branching by the Arp2/3 complex and severing by cofilin, both of which contact regions of the actin protomer that are structurally altered by αE-catenin ABD binding. In epithelial cells, there is little correlation between the distribution of αE-catenin and the Arp2/3 complex at developing cell-cell contacts. Our results indicate that αE-catenin binding to filamentous actin favors assembly of unbranched filament bundles that are protected from severing over more dynamic, branched filament arrays.

https://pubmed.ncbi.nlm.nih.gov/24068324