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

17 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
Externally publishedYes

Keywords

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

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology

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