Physical and functional interactions between ZIP kinase and UbcH5

Norihiko Ohbayashi, Katsuya Okada, Shiho Kawakami, Sumihito Togi, Noriko Sato, Osamu Ikeda, Shinya Kamitani, Ryuta Muromoto, Yuichi Sekine, Taro Kawai, Shizuo Akira, Tadashi Matsuda

研究成果: Article査読

4 被引用数 (Scopus)

抄録

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. In our previous study, we showed that leukemia inhibitory factor stimulated threonine-265 phosphorylation of ZIPK, thereby leading to phosphorylation and activation of signal transducer and activator of transcription 3. Here, we identified UbcH5c as a novel ZIPK-binding partner by yeast two-hybrid screening. Importantly, we found that UbcH5c induced ubiquitination of ZIPK. Small-interfering RNA-mediated reduction of endogenous UbcH5 expression decreased ZIPK ubiquitination. Furthermore, coexpression of UbcH5c with ZIPK influenced promyelocytic leukemia protein nuclear body (PML-NB) formation. These results suggest that UbcH5 regulates ZIPK accumulation in PML-NBs by interacting with ZIPK and stimulating its ubiquitination.

本文言語English
ページ(範囲)708-712
ページ数5
ジャーナルBiochemical and biophysical research communications
372
4
DOI
出版ステータスPublished - 2008 8月 8
外部発表はい

ASJC Scopus subject areas

  • 生物理学
  • 生化学
  • 分子生物学
  • 細胞生物学

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