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Physical and functional interactions between ZIP kinase and UbcH5

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Title: Physical and functional interactions between ZIP kinase and UbcH5
Other Titles: Interactions between ZIPK with UbcH5
Authors: Ohbayashi, Norihiko Browse this author
Okada, Katsuya Browse this author
Kawakami, Shiho Browse this author
Togi, Sumihito Browse this author
Sato, Noriko Browse this author
Ikeda, Osamu Browse this author
Kamitani, Shinya Browse this author
Muromoto, Ryuta Browse this author
Sekine, Yuichi Browse this author
Kawai, Taro Browse this author
Akira, Shizuo Browse this author
Matsuda, Tadashi Browse this author →KAKEN DB
Keywords: ZIPK
PML nuclear body
Issue Date: 8-Aug-2008
Publisher: Academic Press
Journal Title: Biochemical and Biophysical Research Communications
Volume: 372
Issue: 4
Start Page: 708
End Page: 712
Publisher DOI: 10.1016/j.bbrc.2008.05.113
PMID: 18515077
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.
Type: article (author version)
Appears in Collections:薬学研究院 (Faculty of Pharmaceutical Sciences) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 松田 正

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