کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2051853 | 1074211 | 2006 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Negative regulation of protein phosphatase 2Cβ by ISG15 conjugation
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
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.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: FEBS Letters - Volume 580, Issue 18, 7 August 2006, Pages 4521–4526
Journal: FEBS Letters - Volume 580, Issue 18, 7 August 2006, Pages 4521–4526
نویسندگان
Tomoharu Takeuchi, Takayasu Kobayashi, Shinri Tamura, Hideyoshi Yokosawa,