The adhesion modulation domain of C. elegans α-catenin regulates actin binding during morphogenesis.

The adhesion modulation domain of C. elegans α-catenin regulates actin binding during morphogenesis. Mol Biol Cell. 2019 Jun 12;:mbcE19010018 Authors: Shao X, Lucas B, Strauch J, Hardin J Abstract Maintaining tissue integrity during epidermal morphogenesis depends on α-catenin, which connects the cadherin complex to F-actin. We show that the adhesion modulation domain (AMD) of C. elegans HMP-1/α-catenin regulates its F-actin binding activity and organization of junctional proximal actin in vivo. Deleting the AMD increases F-actin binding in vitro and leads to excess actin recruitment to adherens junctions in vivo. Reducing actin binding through a compensatory mutation in the C terminus leads to improved function. Based on the effects of phosphomimetic and non-phosphorylatable mutations phosphorylation of S509, within the AMD, may regulate F-actin binding. Taken together, these data establish a novel role for the AMD in regulating the actin binding ability of an α-catenin and its proper function during epithelial morphogenesis. PMID: 31188702 [PubMed - as supplied by publisher]
Source: Mol Biol Cell - Category: Molecular Biology Authors: Tags: Mol Biol Cell Source Type: research