Phosphorylation of myosin II regulatory light chain by ZIP kinase is responsible for cleavage furrow ingression during cell division in mammalian cultured cells

Biochemical and Biophysical Research Communications
Kosuke HosobaKozue Hamao

Abstract

Zipper-interacting protein kinase (ZIPK) is known to regulate several functions such as apoptosis, smooth muscle contraction, and cell migration. While exogenously expressed GFP-ZIPK localizes to the cleavage furrow, role of ZIPK in cytokinesis is obscure. Here, we show that ZIPK is a major MRLC kinase during mitosis. Moreover, ZIPK siRNA-mediated knockdown causes delay of cytokinesis. The delay in cytokinesis of ZIPK-knockdown cells was rescued by the exogenous diphosphorylation-mimicking MRLC mutant. Taken together, these findings suggest that ZIPK plays a role in the progression and completion of cytokinesis through MRLC phosphorylation.

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Citations

Jun 11, 2019·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·Yiteng ZhangHuaqun Chen
Oct 10, 2020·Biochemical and Biophysical Research Communications·Taichiro OnoKozue Hamao
Jul 28, 2021·Annual Review of Cell and Developmental Biology·Marina Garrido-CasadoMiguel Vicente-Manzanares

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