Abstract
During epithelial sheet formation, linear actin cables assemble at nascent adherens junctions. This process requires α-catenin and actin polymerization, although the underlying mechanism is poorly understood. Here, we show that formin-1 interacts with α-catenin, localizes to adherens junctions and nucleates unbranched actin filaments. Furthermore, disruption of the α-catenin–formin-1 interaction blocks assembly of radial actin cables and perturbs intercellular adhesion. A fusion protein of the β-catenin-binding domain of α-catenin with the actin polymerization domains of formin-1 rescues formation of adherens junctions and associated actin cables in α-catenin-null keratinocytes. These findings provide new insight into how α-catenin orchestrates actin dynamics during intercellular junction formation.
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Acknowledgements
E.F. is an investigator of the Howard Hughes Medical Institute. We thank V. Vasioukhin for valuable discussions in the early stages of this work, W. Lowry for assistance with the actin polymerization studies, A. North and A. Vaezi for their assistance with Deltavision imaging, and P. Leder, A. Alberts, S. Narumiya and L. Cantley for reagents. This work was supported by the National Institutes of Health (RO1-AR27883 to E. F.) and the Howard Hughes Medical Institute.
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Kobielak, A., Pasolli, H. & Fuchs, E. Mammalian formin-1 participates in adherens junctions and polymerization of linear actin cables. Nat Cell Biol 6, 21–30 (2004). https://doi.org/10.1038/ncb1075
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DOI: https://doi.org/10.1038/ncb1075
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