Phosphorylation of myosin II regulatory light chain by ZIP kinase is responsible for cleavage furrow ingression during cell division in mammalian cultured cells.
Phosphorylation of myosin II regulatory light chain by ZIP kinase is responsible for cleavage furrow ingression during cell division in mammalian cultured cells.
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DOI：
10.1016/j.bbrc.2015.03.005
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发表时间：
2015-04-17
影响因子：
3.1
通讯作者：
Hamao, Kozue
中科院分区：
文献类型：
--
作者：
Hosoba, Kosuke;Komatsu, Satoshi;Ikebe, Mitsuo;Kotani, Manato;Xiao Wenqin;Tachibana, Taro;Hosoya, Hiroshi;Hamao, Kozue
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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影响因子：
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Okuno, M
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