RT Journal Article
SR Electronic
T1 CLIC4 and CLIC1 bridge plasma membrane and cortical actin network for a successful cytokinesis
JF Life Science Alliance
JO Life Sci. Alliance
FD Life Science Alliance LLC
SP e201900558
DO 10.26508/lsa.201900558
VO 3
IS 2
A1 Uretmen Kagiali, Zeynep Cansu
A1 Saner, Nazan
A1 Akdag, Mehmet
A1 Sanal, Erdem
A1 Degirmenci, Beste Senem
A1 Mollaoglu, Gurkan
A1 Ozlu, Nurhan
YR 2020
UL http://www.life-science-alliance.org/content/3/2/e201900558.abstract
AB 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, and ALIX are identified as interaction partners of CLIC4 at the cleavage furrow and midbody. Strikingly, CLIC4 facilitates the activation of ezrin at the cleavage furrow and reciprocally inhibition of ezrin activation diminishes the translocation of CLIC4 to the cleavage furrow. Furthermore, knockouts of CLIC4 and CLIC1 cause abnormal blebbing at the polar cortex and regression of the cleavage furrow at late cytokinesis leading to multinucleated cells. We conclude that CLIC4 and CLIC1 function together with ezrin where they bridge plasma membrane and actin cytoskeleton at the polar cortex and cleavage furrow to promote cortical stability and successful completion of cytokinesis in mammalian cells.