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Negative regulation of protein phosphatase 2Cβ by ISG15 conjugation

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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
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.
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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: 横沢 英良

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