The adhesion modulation domain of Caenorhabditis elegans α-catenin regulates actin binding during morphogenesis
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 HMP-1/α-catenin regulates its F-actin-binding activity and organization of junctional-proximal actin in vivo. Deletin...
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| Veröffentlicht in: | Molecular biology of the cell 2019-08, Vol.30 (17), p.2115-2123 |
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| creator | Shao, Xiangqiang Lucas, Bethany Strauch, Jared Hardin, Jeff |
| description | 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
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. |
| doi_str_mv | 10.1091/mbc.E19-01-0018 |
| format | Article |
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| title | The adhesion modulation domain of Caenorhabditis elegans α-catenin regulates actin binding during morphogenesis |
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