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Anillin regulates cell‐cell junction integrity by organizing junctional accumulation of RhoA‐GTP, F‐actin, and Myosin‐2 (1109.17)

Anillin is a scaffolding protein that organizes and stabilizes actomyosin contractile rings and was previously thought to function primarily in cytokinesis. 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. Further, 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 abnormal intercellular spaces and increased permeability to fluorescent dextran. Further, fluorescence recover after photobleaching (FRAP) studies show that Anillin perturbation affects the dynamics of the tight junction protein ZO‐1. Anillin interacts with RhoA, F‐actin, and Myosin‐2, all of which regulate cell‐cell junction structure and function. When Anillin is knocked down, active RhoA (RhoA‐GTP), F‐actin, and Myosin‐2 are misregulated at junctions. Indeed, while overall accumulation of RhoA‐GTP is reduced when Anillin is depleted, increased dynamic “flares” of RhoA‐GTP are observed at cell‐cell junctions. Junctional accumulation of F‐actin and Myosin‐2 are also reduced when Anillin is depleted. We propose that Anillin is required for proper RhoA‐GTP distribution at cell‐cell junctions in order to maintain 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.