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

  title={ZIP kinase identified as a novel myosin regulatory light chain kinase in HeLa cells},
  author={Maki Murata-Hori and Futoshi Suizu and Takahiro Iwasaki and Alexander Kikuchi and Hiroshi Hosoya},
  journal={FEBS Letters},

Inhibition of zipper-interacting protein kinase function in smooth muscle by a myosin light chain kinase pseudosubstrate peptide.

It is concluded that the SM1 peptide, which has no effect on ILK, can be used to distinguish between ZIPK and ILK effects in smooth muscle tissues.

ZIP kinase is responsible for the phosphorylation of myosin II and necessary for cell motility in mammalian fibroblasts

The results suggest that zipper-interacting protein (ZIP) kinase is critical for myosin phosphorylation and necessary for cell motile processes in mammalian fibroblasts.

Zipper-interacting Protein Kinase Induces Ca2+-free Smooth Muscle Contraction via Myosin Light Chain Phosphorylation*

Cloned smooth muscle zipper-interacting protein (ZIP) kinase cDNA is cloned and it is suggested that ZIP kinase is responsible for Ca2+ independent myosin phosphorylation and contraction in smooth muscle.

Phosphorylation of the myosin phosphatase target subunit by integrin-linked kinase.

The findings that ILK phosphorylated both MYPT1 and myosin and the association of ILK with MP suggest thatILK may influence cytoskeletal structure or function.

Vascular smooth muscle myosin light chain diphosphorylation: Mechanism, function, and pathological implications

Kinases such as ILK, ROCK, and ZIPK are potential therapeutic targets in the treatment of, for example, cerebral vasospasm following subarachnoid hemorrhage and atherosclerosis.

ROCK1 Phosphorylates and Activates Zipper-interacting Protein Kinase*

These findings provide a new regulatory pathway in smooth muscle and non-muscle cells whereby ROCK1 phosphorylates and regulates ZIP kinase.

Solution NMR structure of the myosin phosphatase inhibitor protein CPI-17 shows phosphorylation-induced conformational changes responsible for activation.

Chemical shift perturbations indicated that phosphorylation of Thr38 induces a conformational change involving displacement of helix A, without significant movement of the other three helices, which offers new structural insights toward understanding the specificity of CPI-17 for myosin phosphatase and its function as a molecular switch.



Mitosis-specific phosphorylation of myosin light chain kinase.

Isolation of cDNA for bovine stomach 155 kDa protein exhibiting myosin light chain kinase activity.

The deduced amino acid sequence revealed a high degree of similarity to those of chicken and rabbit smooth muscle myosin light chain kinases, suggesting that the 155 kDa protein has additional functions other than its enzymatic activity.

Phosphorylation of a second site for myosin light chain kinase on platelet myosin.

  • M. Ikebe
  • Chemistry, Biology
  • 1989
The results suggest that the phosphorylation at the threonine residue as well as at the serine residue may play an important role in the contractility of nonmuscle cells.

Phosphorylation and Activation of Myosin by Rho-associated Kinase (Rho-kinase)*

The phosphorylation of MLC by Rho-kinase resulted in the facilitation of the actin activation of myosin ATPase, which may partly account for the mechanism by which Rho regulates cytokinesis, cell motility, or smooth muscle contraction.

Specific Localization of Serine 19 Phosphorylated Myosin II during Cell Locomotion and Mitosis of Cultured Cells

Observations suggest that peripheral microfilaments at the edge are involved in force production to drive the cell margin forward while microfilament bundles in cell–cell contacts play a structural role.

ZIP Kinase, a Novel Serine/Threonine Kinase Which Mediates Apoptosis

The catalytic domain of ZIP kinase is closely related to that of death-associated protein kinase (DAP kinase), which is a mediator of apoptosis induced by gamma interferon, therefore, both ZIP and DAP kinases represent a novel kinase family, which mediates apoptosis through their catalytic activities.

Cloning and characterization of Dlk, a novel serine/threonine kinase that is tightly associated with chromatin and phosphorylates core histones

Dlk seems to be tightly associated with insoluble nuclear structures, presumably chromatin, since it was resistant to various rigorous extraction procedures but it was partially released upon DNase I digestion of nuclei.

DAP‐kinase is a Ca2+/calmodulin‐dependent, cytoskeletal‐associated protein kinase, with cell death‐inducing functions that depend on its catalytic activity

DAP‐kinase is therefore a novel cytoskeletal‐associated cell death serine/threonine kinase whose activation by Ca2+/calmodulin may be linked to the biochemical mechanism underlying the cytOSkeletal alterations that occur during cell death.