Novel ZIP kinase isoform lacks leucine zipper
作者： Norio Takamoto , Satoshi Komatsu , Shigeru Komaba , Naohisa Niiro , Mitsuo Ikebe
DOI: 10.1016/J.ABB.2006.09.026
关键词:
摘要: 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 also plays a role regulating myosin phosphorylation. Here, we found novel isoform which non-kinase domain containing eliminated (hZIPK-S). hZIPK-S binds phosphatase targeting subunit 1(MYPT1) similar long (hZIPK-L). In addition, as well hZIPK-L bind myosin. These results indicate not critical binding of MYPT1 Consistently, localized with stress-fibers where they co-localized The residues 278-311, side common both isoforms, MYPT1, while within domain. suggest newly play an regulation
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