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    FEBS Lett. 1999 May 14;451(1):81-4.

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

    Murata-Hori M, Suizu F, Iwasaki T, Kikuchi A, Hosoya H.

    Source

    Department of Biological Science, Faculty of Science, Hiroshima University, Higashi-Hiroshima, Japan.

    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.

    PMID:
    10356987
    [PubMed - indexed for MEDLINE]

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