Current Biology
Volume 24, Issue 11, 2 June 2014, Pages 1263-1270
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Anillin Regulates Cell-Cell Junction Integrity by Organizing Junctional Accumulation of Rho-GTP and Actomyosin

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Highlights

  • Anillin localizes to epithelial cell-cell junctions throughout the cell cycle

  • Anillin is required for proper adherens junction and tight junction structure

  • Anillin depletion results in altered cell shape and increased intercellular spaces

  • Anillin regulates Rho-GTP localization and stabilizes the apical actomyosin belt

Summary

Anillin is a scaffolding protein that organizes and stabilizes actomyosin contractile rings and was previously thought to function primarily in cytokinesis [1, 2, 3, 4, 5, 6, 7, 8, 9, 10]. Using Xenopus laevis embryos as a model system to examine Anillin’s role in the intact vertebrate epithelium, we find that a population of Anillin surprisingly localizes to epithelial cell-cell junctions throughout the cell cycle, whereas it was previously thought to be nuclear during interphase [5, 11]. Furthermore, we show that Anillin plays a critical role in regulating cell-cell junction integrity. Both tight junctions and adherens junctions are disrupted when Anillin is knocked down, leading to altered cell shape and increased intercellular spaces. Anillin interacts with Rho, F-actin, and myosin II [3, 8, 9], all of which regulate cell-cell junction structure and function. When Anillin is knocked down, active Rho (Rho-guanosine triphosphate [GTP]), F-actin, and myosin II are misregulated at junctions. Indeed, increased dynamic “flares” of Rho-GTP are observed at cell-cell junctions, whereas overall junctional F-actin and myosin II accumulation is reduced when Anillin is depleted. We propose that Anillin is required for proper Rho-GTP distribution at cell-cell junctions and for maintenance of a robust apical actomyosin belt, which is required for cell-cell junction integrity. These results reveal a novel role for Anillin in regulating epithelial cell-cell junctions.

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