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10.1016/j.bbrc.2015.03.005 http://scihub22266oqcxt.onion/10.1016/j.bbrc.2015.03.005 C4402231!4402231 !25769953     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=25769953 &cmd=llinks): Failed to open stream: HTTP request failed! 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Phosphorylation of myosin II regulatory light chain by ZIP kinase is responsible for cleavage furrow ingression during cell division in mammalian cultured cells |pdf=|usr=}}{{25769953 }} gab.com Text Phosphorylation of myosin II regulatory light chain by ZIP kinase is responsible for cleavage furrow ingression during cell division in mammalian cultured cells JO: Biochem Biophys Res Commun http://www.kidney.de/pget.php?&tw=1&pmid=25769953 #FOAvip 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. Twit Text FOAVip 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 http://www.kidney.de/pget.php?&tw=1&pmid=25769953 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25769953 #FOAvip English Wikipedia <ref>{{Cite pmid|25769953 }}</ref> Phosphorylation of myosin II regulatory light chain by ZIP kinase is responsible for cleavage furrow ingression during cell division in mammalian cultured cells #MMPMID25769953 Hosoba K ; Komatsu S ; Ikebe M ; Kotani M ; Wenqin X ; Tachibana T ; Hosoya H ; Hamao K Biochem Biophys Res Commun 2015[Apr]; 459 (4 ): 686-91 PMID25769953 show ga 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. |*Cell Division [MESH] |Cell Line [MESH] |Death-Associated Protein Kinases/genetics/*metabolism [MESH] |Humans [MESH] |Myosin Type II/*metabolism [MESH] |Phosphorylation [MESH]Phosphorylation of myosin II regulatory light chain by ZIP kinase is r(epmc).pdf DeepDyve Pubget Overpricing