Physical and functional interactions between ZIP kinase and UbcH5

• Ohbayashi, Norihiko

• Okada, Katsuya

• Kawakami, Shiho

• Togi, Sumihito

• Sato, Noriko

• Ikeda, Osamu

• Kamitani, Shinya

• Muromoto, Ryuta

• Sekine, Yuichi

• Kawai, Taro

• Akira, Shizuo

• Matsuda, Tadashi

Bibliographic Information

Other Title

• Interactions between ZIPK with UbcH5

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.

Journal

• Biochemical and Biophysical Research Communications

  Biochemical and Biophysical Research Communications 372 (4), 708-712, 2008-08-08

  Academic Press

Keywords

• ZIPK
• UbcH5
• ubiquitination
• PML nuclear body

Details

• CRID: 1050564288949787520
• NII Article ID: 120000952720
• NII Book ID: AA00564395
• ISSN: 10902104
• ISSN: 0006291X
• HANDLE: 2115/33898
• Text Lang: en
• Article Type: journal article
• Data Source:
  • IRDB
  • CiNii Articles