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Negative regulation of protein phosphatase 2Cβ by ISG15 conjugation

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タイトル: Negative regulation of protein phosphatase 2Cβ by ISG15 conjugation
著者: Takeuchi, Tomoharu 著作を一覧する
Kobayashi, Takayasu 著作を一覧する
Tamura, Shinri 著作を一覧する
Yokosawa, Hideyoshi 著作を一覧する
キーワード: Interferon-stimulated gene 15 kDa
Interferon
Ubiquitin
Protein phosphatase
Nuclear factor κB
発行日: 2006年 8月 7日
出版者: Federation of European Biochemical Societies Published by Elsevier B.V.
誌名: FEBS Letters
巻: 580
号: 18
開始ページ: 4521
終了ページ: 4526
出版社 DOI: 10.1016/j.febslet.2006.07.032
抄録: 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
資料タイプ: article (author version)
URI: http://hdl.handle.net/2115/14658
出現コレクション:雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

提供者: 横沢 英良

 

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