Novel ZIP kinase isoform lacks leucine zipper.

Article Details

Citation

Takamoto N, Komatsu S, Komaba S, Niiro N, Ikebe M

Novel ZIP kinase isoform lacks leucine zipper.

Arch Biochem Biophys. 2006 Dec 15;456(2):194-203. Epub 2006 Oct 16.

PubMed ID
17126281 [ View in PubMed
]
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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Death-associated protein kinase 3O43293Details