Physical and functional interactions between ZIP kinase and UbcH5
| Autor: | Taro Kawai, Noriko Sato, Osamu Ikeda, Shinya Kamitani, Tadashi Matsuda, Yuichi Sekine, Shizuo Akira, Katsuya Okada, Norihiko Ohbayashi, Sumihito Togi, Ryuta Muromoto, Shiho Kawakami |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2008 |
| Předmět: |
Biophysics
Promyelocytic Leukemia Protein Biology ubiquitination Biochemistry ZIPK UbcH5 Promyelocytic leukemia protein Ubiquitin Two-Hybrid System Techniques Transcriptional regulation Humans RNA Small Interfering Protein kinase A Molecular Biology Cell Nucleus Regulation of gene expression Kinase Tumor Suppressor Proteins PML nuclear body Nuclear Proteins Cell Biology Death-Associated Protein Kinases Calcium-Calmodulin-Dependent Protein Kinases Ubiquitin-Conjugating Enzymes Cancer research biology.protein STAT protein Phosphorylation Apoptosis Regulatory Proteins HeLa Cells Transcription Factors |
| Zdroj: | Biochemical and Biophysical Research Communications. 372(4):708-712 |
| ISSN: | 0006-291X |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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