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

Research output: Contribution to journalArticlepeer-review

4 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. 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.

Original languageEnglish
Pages (from-to)708-712
Number of pages5
JournalBiochemical and biophysical research communications
Volume372
Issue number4
DOIs
Publication statusPublished - 2008 Aug 8
Externally publishedYes

Keywords

  • PML nuclear body
  • UbcH5
  • Ubiquitination
  • ZIPK

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint

Dive into the research topics of 'Physical and functional interactions between ZIP kinase and UbcH5'. Together they form a unique fingerprint.

Cite this