Monomeric α-catenin links cadherin to the actin cytoskeleton
| Autor: | Milena Pellikka, Ritu Sarpal, Ulrich Tepass, Mitsuhiko Ikura, Ridhdhi Desai, Noboru Ishiyama |
|---|---|
| Rok vydání: | 2013 |
| Předmět: |
Cytoplasm
Embryo Nonmammalian Immunoblotting Arp2/3 complex macromolecular substances Epithelium Immunoenzyme Techniques Adherens junction Allosteric Regulation Cell Adhesion Image Processing Computer-Assisted Animals Immunoprecipitation Cell adhesion Cytoskeleton Cells Cultured beta Catenin biology Chemistry Cadherin Cell Membrane Gene Expression Regulation Developmental Adherens Junctions Cell Biology Cadherins Actin cytoskeleton Actins Cell biology Actin Cytoskeleton Drosophila melanogaster Profilin Catenin Mutation biology.protein Protein Multimerization alpha Catenin |
| Zdroj: | Nature Cell Biology. 15:261-273 |
| ISSN: | 1476-4679 1465-7392 |
| Popis: | The linkage of adherens junctions to the actin cytoskeleton is essential for cell adhesion. The contribution of the cadherin-catenin complex to the interaction between actin and the adherens junction remains an intensely investigated subject that centres on the function of α-catenin, which binds to cadherin through β-catenin and can bind F-actin directly or indirectly. Here, we delineate regions within Drosophila α-Catenin (α-Cat) that are important for adherens junction performance in static epithelia and dynamic morphogenetic processes. Moreover, we address whether persistent α-catenin-mediated physical linkage between cadherin and F-actin is crucial for cell adhesion and characterize the functions of α-catenin monomers and dimers at adherens junctions. Our data support the view that monomeric α-catenin acts as an essential physical linker between the cadherin-β-catenin complex and the actin cytoskeleton, whereas α-catenin dimers are cytoplasmic and form an equilibrium with monomeric junctional α-catenin. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|