Negative regulation of protein phosphatase 2Cβ by ISG15 conjugation

Takeuchi, Tomoharu; Kobayashi, Takayasu; Tamura, Shinri; Yokosawa, Hideyoshi

Negative regulation of protein phosphatase 2Cβ by ISG15 conjugation

Takeuchi, Tomoharu; Kobayashi, Takayasu; Tamura, Shinri et al.

FEBS Letters, 2006, 580(18), 4521-4526

Permalink : https://hdl.handle.net/2115/14658

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アクセス権	open access
URI	https://hdl.handle.net/2115/14658
タイトル	Negative regulation of protein phosphatase 2Cβ by ISG15 conjugation
著者	Takeuchi, Tomoharu ; Kobayashi, Takayasu ; Tamura, Shinri ; Yokosawa, Hideyoshi
著者名 Takeuchi, Tomoharu
著者名 Kobayashi, Takayasu
著者名 Tamura, Shinri
著者名 Yokosawa, Hideyoshi
言語	英語
キーワード	Interferon-stimulated gene 15 kDa
	Interferon
	Ubiquitin
	Protein phosphatase
	Nuclear factor κB
発行日	2006-08-07
出版者	Federation of European Biochemical Societies Published by Elsevier B.V.
収録物名	FEBS Letters
巻(号)	580(18)
ページ	4521-4526
記述	http://www.elsevier.com/wps/find/journaldescription.cws_home/506085/description
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.
資源タイプ	学術雑誌論文
出版タイプ	Accepted Manuscript
PISSN	0014-5793
関連情報	PMID 16872604
関連情報 (isVersionOf)	出版社版DOI https://doi.org/10.1016/j.febslet.2006.07.032