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

Biochem Biophys Res Commun. 2015 Apr 17;459(4):686-91. doi: 10.1016/j.bbrc.2015.03.005. Epub 2015 Mar 11.

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.

Keywords: Cytokinesis; Myosin II regulatory light chain; ZIP kinase.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Division*
  • Cell Line
  • Death-Associated Protein Kinases / genetics
  • Death-Associated Protein Kinases / metabolism*
  • Humans
  • Myosin Type II / metabolism*
  • Phosphorylation
  • RNA, Small Interfering / genetics

Substances

  • RNA, Small Interfering
  • Death-Associated Protein Kinases
  • Myosin Type II