Phosphorylation of threonine-265 in Zipper-interacting protein kinase plays an important role in its activity and is induced by IL-6 family cytokines

Noriko Sato, Nobuyuki Kamada, Ryuta Muromoto, Taro Kawai, Kenji Sugiyama, Tadashi Watanabe, Seiyu Imoto, Yuichi Sekine, Norihiko Ohbayashi, Masato Ishida, Shizuo Akira, Tadashi Matsuda

    Research output: Contribution to journalArticlepeer-review

    15 Citations (Scopus)

    Abstract

    Zipper-interacting protein kinase (ZIPK) is a widely expressed serine/threonine kinase that has been implicated in cell death and transcriptional regulation, but its mechanism of regulation remains unknown. Here, we identified threonine-265 (Thr265) in ZIPK as a major autophosphorylation site. Mutational analyses revealed that autophosphorylation of Thr265 were essential for its full catalytic activity toward an exogenous substrate as well as for cell death induction. Furthermore, leukemia inhibitory factor (LIF) stimulated Thr265 phosphorylation of ZIPK, thereby leading to phosphorylation and activation of signal transducer and activator of transcription (STAT3). Taken together, our findings demonstrate that ZIPK is positively regulated through Thr265 phosphorylation and that this phosphorylation is essential for its function.

    Original languageEnglish
    Pages (from-to)127-134
    Number of pages8
    JournalImmunology Letters
    Volume103
    Issue number2
    DOIs
    Publication statusPublished - 2006 Mar 15

    Keywords

    • Apoptosis
    • IL-6
    • LIF
    • Phosphorylation
    • ZIPK

    ASJC Scopus subject areas

    • Immunology and Allergy
    • Immunology

    Fingerprint Dive into the research topics of 'Phosphorylation of threonine-265 in Zipper-interacting protein kinase plays an important role in its activity and is induced by IL-6 family cytokines'. Together they form a unique fingerprint.

    Cite this