Cell division is completed after execution of cytokinesis, during which the cleavage furrow forms an intercellular bridge that, once resolved, separates the two daughter cells. Cell shape changes and cytoskeleton remodelling are involved in this transition, but new regulatory proteins responsible for these cytoskeletal alterations are still being discovered. In their study, Rytis Prekeris and colleagues (Peterman et al., 2020) identify chloride intracellular channel 4 (CLIC4) as a regulator of the cortical cytoskeleton regulator during cell division. The authors show that CLIC4 is enriched in the cytokinetic furrow in a RhoA GTPase-dependent manner. CLIC4 knockdown results in cytokinesis defects, ranging from increased mitotic time, with blebbing at the ingression site, to furrow regression and polyploidy. Moreover, removing CLIC4 from the furrow with the use of optogenetic tools causes similar phenotypes. The authors also observe decreased levels of cortical actin, non-muscle myosin II and ezrin, a member of the ezrin–radixin–moesin (ERM) family of proteins, at the furrow in the absence of CLIC4, which suggests these phenotypes are due to weaker cortical tension. Finally, they show that CLIC4, together with anillin, recruits the MST4 kinase, which is responsible for ezrin activation during cytokinesis. This work thus uncovers a new role for CLIC4, independent of its chloride channel function, in the regulation of cytoskeletal dynamics and cortical stability during cell division.
CLIC4 actin’ in cytokinesis
CLIC4 actin’ in cytokinesis. J Cell Sci 1 May 2020; 133 (9): e0903. doi:
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