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Negative regulation of protein phosphatase 2Cβ by ISG15 conjugation
| Title: | Negative regulation of protein phosphatase 2Cβ by ISG15 conjugation |
| Authors: | Takeuchi, Tomoharu Browse this author | | Kobayashi, Takayasu Browse this author | | Tamura, Shinri Browse this author | | Yokosawa, Hideyoshi Browse this author |
| Keywords: | Interferon-stimulated gene 15 kDa | | Interferon | | Ubiquitin | | Protein phosphatase | | Nuclear factor κB |
| Issue Date: | 7-Aug-2006 |
| Publisher: | Federation of European Biochemical Societies Published by Elsevier B.V. |
| Journal Title: | FEBS Letters |
| Volume: | 580 |
| Issue: | 18 |
| Start Page: | 4521 |
| End Page: | 4526 |
| Publisher DOI: | 10.1016/j.febslet.2006.07.032 |
| PMID: | 16872604 |
| Abstract: | ISG15, an interferon-upregulated ubiquitin-like protein, is covalently conjugated to various cellular proteins (ISGylation). In this study, we found that protein phosphatase 2Cβ (PP2Cβ), which functions in the nuclear factor κB (NF-κB) pathway via dephosphorylation of TGF-β-activated kinase, was ISGylated, and analysis by NF-κB luciferase reporter assay revealed that PP2Cβ activity was suppressed by co-expression of ISG15, UBE1L, and UbcH8. We determined the ISGylation sites of PP2Cβ and constructed its ISGylation-resistant mutant. In contrast to the wild type, this mutant suppressed the NF-κB pathway even in the presence of ISG15, UBE1L, and UbcH8. Thus, we propose that ISGylation negatively regulates PP2Cβ activity. |
| Description URI: | http://www.elsevier.com/wps/find/journaldescription.cws_home/506085/description |
| Type: | article (author version) |
| URI: | http://hdl.handle.net/2115/14658 |
| Appears in Collections: | 薬学研究院 (Faculty of Pharmaceutical Sciences) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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Submitter: 横沢 英良
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