ArticleArchives of biochemistry and biophysics2006
Novel ZIP kinase isoform lacks leucine zipper.
Article in Archives of biochemistry and biophysics, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Kinetic Scheme of Myosin Phosphorylation by ZIP Kinase.Biochemistry · 2025Article
- Identification of Novel Death-Associated Protein Kinase 2 Interaction Partners by Proteomic Screening Coupled with Bimolecular Fluorescence Complementation.Molecular and cellular biology · 2016Article
- Localization of myosin 1b to actin protrusions requires phosphoinositide binding.The Journal of biological chemistry · 2010Article
- Par-4 is an essential downstream target of DAP-like kinase (Dlk) in Dlk/Par-4-mediated apoptosis.Molecular biology of the cell · 2009Article
- ZIPK: a unique case of murine-specific divergence of a conserved vertebrate gene.PLoS genetics · 2007Article
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Authors and funding
5 authors.
Funding
Abstract
Zipper-interacting protein kinase (ZIP kinase) has been thought to be involved in apoptosis and the C-terminal leucine zipper motif is important for its function. Recent studies have revealed that ZIP kinase also plays a role in regulating myosin phosphorylation. Here, we found novel ZIP kinase isoform in which the C-terminal non-kinase domain containing a leucine zipper is eliminated (hZIPK-S). hZIPK-S binds to myosin phosphatase targeting subunit 1(MYPT1) similar to the long isoform (hZIPK-L). In addition, we found that hZIPK-S as well as hZIPK-L bind to myosin. These results indicate that a leucine zipper is not critical for the binding of ZIP kinase to MYPT1 and myosin. Consistently, hZIPK-S localized with stress-fibers where they co-localized with myosin. The residues 278-311, the C-terminal side of the kinase domain common to the both isoforms, is involved in the binding to MYPT1, while the myosin binding domain is within the kinase domain. These results suggest that the newly found hZIPK-S as well as the long isoform play an important role in the regulation of myosin phosphorylation.
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Registered trials
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