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A more recent version of this article appeared on December 1, 2002
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Submitted on April 26, 2002
Revised on July 24, 2002
Accepted on August 22, 2002
1 Gene Function Research Laboratory, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba, Ibaraki 305-8562, Japan
2 Department of Biology, Faculty of Science,Yamaguchi University, Yamaguchi 753-8512, Japan
* Corresponding author. E-mail address: a-nagasaki{at}aist.go.jp.
We have cloned a full-length cDNA encoding a novel myosin II heavy chain kinase (mhckC) from Dictyostelium. Like other members of the myosin heavy chain kinase family, the mhckC gene product, MHCK C, has a kinase domain in its N terminal half and six WD repeats in the C terminal half. GFP-MHCK C fusion protein localized to the cortex of interphase cells, to the cleavage furrow of mitotic cells, and to the posterior of migrating cells. These distributions of GFP-MHCK C always corresponded with that of myosin II filaments and were not observed in myosin II-nullcells, where GFP-MHCK C was diffusely distributed in the cytoplasm. Thus, localization of MHCK C appears to be myosin II-dependent. Cells lacking the mhckC gene exhibited excessive aggregation of myosin II filaments in the cleavage furrows and in the posteriors of the daughter cells once cleavage was complete. The cleavage process of these cells took longer time than wild-type cells. Taken together, these findings suggest MHCK C drives the disassembly of myosin II filaments for efficient cytokinesis and recycling of myosin II that occurs during cytokinesis.
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