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Updated: Jan 23, 2026

Measuring Protein Binding to F-actin by Co-sedimentation
Published on: May 18, 2017
The adhesion modulation domain of Caenorhabditis elegans α-catenin regulates actin binding during morphogenesis
Xiangqiang Shao1, Bethany Lucas2, Jared Strauch3
1Program in Genetics, University of Wisconsin-Madison, Madison, WI 53706.
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 Caenorhabditis 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 nonphosphorylatable 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.
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