RRC ID 58579
著者 Hamao K, Ono T, Matsushita M, Hosoya H.
タイトル ZIP kinase phosphorylated and activated by Rho kinase/ROCK contributes to cytokinesis in mammalian cultured cells.
ジャーナル Exp Cell Res
Abstract Cytokinesis of animal cells requires contraction of a contractile ring, composed of actin filaments and myosin II filaments. Phosphorylation of myosin II regulatory light chain (MRLC) promotes contraction of the actomyosin ring by activating myosin II motor activity. Both Rho-associated coiled-coil kinase (Rho kinase/ROCK) and Zipper-interacting protein kinase (ZIP kinase/ZIPK) have been reported to phosphorylate MRLC at the contractile ring. However, it remains unclear whether these kinases function independently of each other. Here, we clarified that ROCK colocalizes and forms a complex with ZIPK at telophase. As ROCK is reported to phosphorylate and activate ZIPK in vitro, we hypothesized that ZIPK phosphorylated by ROCK contributes to control cytokinesis. To address this, we expressed EGFP-ZIPK wild type (WT), a non-phosphorylatable mutant (T265A) or a phosphorylation-mimicking mutant (T265D) in HeLa cells and treated these cells with a ROCK inhibitor. Decrease in phosphorylated MRLC and a delay of furrow ingression by the ROCK inhibitor were rescued by the expression of EGFP-ZIPK-T265D, but not EGFP-ZIPK-WT or -T265A. This suggests that ROCK regulates MRLC phosphorylation followed by furrow ingression, through ZIPK phosphorylation.
巻・号 386(1)
ページ 111707
公開日 2020-1-1
DOI 10.1016/j.yexcr.2019.111707
PII S0014-4827(19)30586-5
PMID 31693874
MeSH Cytokinesis* Death-Associated Protein Kinases / genetics Death-Associated Protein Kinases / metabolism* HeLa Cells Humans Loss of Function Mutation Myosin Light Chains / metabolism Phosphorylation rho-Associated Kinases / metabolism*
IF 3.383
引用数 1
リソース情報
ヒト・動物細胞 HeLa(RCB0007)