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Resolving the cadherin–F-actin connection

Nature Cell Biology volume 19, pages 14–16 (2017)Cite this article

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Cadherin adhesion complexes have recently emerged as sensors of tissue tension that regulate key developmental processes. Super-resolution microscopy experiments now unravel the spatial organization of the interface between cadherins and the actin cytoskeleton and reveal how vinculin, a central component in cadherin mechanotransduction, is regulated by mechanical and biochemical signals.

Tensional forces in cells and tissues, generated by the actomyosin cytoskeleton and coupled to sites of cell adhesion, are crucial for the cell shape changes that occur during morphogenesis, as well as for the coordinated regulation of cell growth and differentiation1. Recently, the cadherin adhesion complex was identified as the mechanosensor at cell–cell junctions that transduces changes in tissue tension into biochemical signals to control the above processes2. This has spurred an interest in understanding the cadherin complex organization to explain its mechanosensitive capabilities. Bertocchi et al. now use super-resolution microscopy to elucidate the architecture of the cadherin/actomyosin interface, providing novel insights into the combined regulation of the central mechanosensitive component vinculin by tension and biochemical signalling3.

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Figure 1: Mechanochemical regulation of vinculin within the cadherin/F-actin interface.

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Authors and Affiliations

  1. Mitchell K. L. Han and Johan de Rooij are at the Molecular Cancer Research, Center for Molecular Medicine, University Medical Center Utrecht, 3584 CG, Utrecht, The Netherlands,

    Mitchell K. L. Han & Johan de Rooij

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  1. Mitchell K. L. Han
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Correspondence to Johan de Rooij.

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Han, M., de Rooij, J. Resolving the cadherin–F-actin connection. Nat Cell Biol 19, 14–16 (2017). https://doi.org/10.1038/ncb3457

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