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

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 ph...

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Bibliographic Details
Published in:FEBS letters 1999-05, Vol.451 (1), p.81-84
Main Authors: Murata-Hori, Maki, Suizu, Futoshi, Iwasaki, Takahiro, Kikuchi, Asako, Hosoya, Hiroshi
Format: Article
Language:English
Subjects:
Actin-activated MgATPase activity
Amino Acid Sequence
Apoptosis Regulatory Proteins
Base Sequence
Calcium-Calmodulin-Dependent Protein Kinases
Cytokinesis
Death-Associated Protein Kinases
DNA, Complementary
HeLa Cells
Humans
Molecular Sequence Data
Myosin light chain kinase
Myosin-Light-Chain Kinase - metabolism
Phosphorylation
Protein-Serine-Threonine Kinases - genetics
Protein-Serine-Threonine Kinases - metabolism
Regulatory light chain of myosin II
Zipper-interacting protein kinase
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Summary: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 Ca 2+/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.
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(99)00550-5