Ontology highlight
ABSTRACT:
SUBMITTER: Uretmen Kagiali ZC
PROVIDER: S-EPMC6933522 | biostudies-literature | 2020 Feb
REPOSITORIES: biostudies-literature
Uretmen Kagiali Zeynep Cansu ZC Saner Nazan N Akdag Mehmet M Sanal Erdem E Degirmenci Beste Senem BS Mollaoglu Gurkan G Ozlu Nurhan N
Life science alliance 20191226 2
CLIC4 and CLIC1 are members of the well-conserved chloride intracellular channel proteins (CLICs) structurally related to glutathione-S-transferases. Here, we report new roles of CLICs in cytokinesis. At the onset of cytokinesis, CLIC4 accumulates at the cleavage furrow and later localizes to the midbody in a RhoA-dependent manner. The cell cycle-dependent localization of CLIC4 is abolished when its glutathione S-transferase activity-related residues (C35A and F37D) are mutated. Ezrin, anillin, ...[more]