Monomeric α-catenin links cadherin to the actin cytoskeleton
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...
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Published in | Nature cell biology Vol. 15; no. 3; pp. 261 - 273 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
London
Nature Publishing Group UK
01.03.2013
Nature Publishing Group |
Subjects | |
Online Access | Get full text |
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Summary: | 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.
Tepass and colleagues use a series of mutant α-catenin forms to study the role of this protein in
Drosophila
in vivo
. Their data support a model in which monomeric α-catenin links the cadherin–β-catenin complex at adherens junction to the actin cytoskeleton. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 1465-7392 1476-4679 |
DOI: | 10.1038/ncb2685 |