Anillin Regulates Cell-Cell Junction Integrity by Organizing Junctional Accumulation of Rho-GTP and Actomyosin
C.C. Reyes, M. Jin, E.B. Breznau, R. Espino, R. Delgado-Gonzalo, A.B. Goryachev, A.L. Miller
Current Biology, vol. 24, no. 11, pp. 1263-1270, June 2, 2014.
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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AUTHOR="Reyes, C.C. and Jin, M. and Breznau, E.B. and Espino, R. and
Delgado-Gonzalo, R. and Goryachev, A.B. and Miller, A.L.",
TITLE="Anillin Regulates Cell-Cell Junction Integrity by Organizing
Junctional Accumulation of Rho-GTP and Actomyosin",
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