ZIP kinase identified as a novel myosin regulatory light chain kinase in HeLa cells

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Abstract

A novel myosin light chain kinase (MLCK) cDNA was isolated from a HeLa cell cDNA library. The deduced amino acid sequence was identical to that of a zipper-interacting protein kinase (ZIPK) which mediates apoptosis [Kawai et al. (1998) Mol. Cell. Biol. 18, 1642-1651]. Here we found that HeLa ZIPK phosphorylated the regulatory light chain of myosin II (MRLC) at both serine 19 and threonine 18 in a Ca2+/calmodulin independent manner. Phosphorylation of myosin II by HeLa ZIPK resulted in activation of actin-activated MgATPase activity of myosin II. HeLa ZIPK is the first non-muscle MLCK that phosphorylates MRLC at two sites. Copyright (C) 1999 Federation of European Biochemical Societies.

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Murata-Hori, M., Suizu, F., Iwasaki, T., Kikuchi, A., & Hosoya, H. (1999). ZIP kinase identified as a novel myosin regulatory light chain kinase in HeLa cells. FEBS Letters, 451(1), 81–84. https://doi.org/10.1016/S0014-5793(99)00550-5

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