| pubmed-article:18775329 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18775329 | lifeskim:mentions | umls-concept:C0003451 | lld:lifeskim |
| pubmed-article:18775329 | lifeskim:mentions | umls-concept:C1335872 | lld:lifeskim |
| pubmed-article:18775329 | lifeskim:mentions | umls-concept:C0521447 | lld:lifeskim |
| pubmed-article:18775329 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:18775329 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:18775329 | lifeskim:mentions | umls-concept:C0205081 | lld:lifeskim |
| pubmed-article:18775329 | lifeskim:mentions | umls-concept:C1158884 | lld:lifeskim |
| pubmed-article:18775329 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:18775329 | pubmed:dateCreated | 2008-9-8 | lld:pubmed |
| pubmed-article:18775329 | pubmed:abstractText | Signal transducers and activators of transcription 1 (STAT1) is activated by tyrosine phosphorylation upon interferon-gamma (IFN-gamma) stimulation. Phosphorylated STAT1 translocates into nucleus to initiate the transcription of IFN-gamma target genes that are important in mediating antiviral, antiproliferative, and immune response. The inactivation of STAT1 is mainly accomplished via tyrosine dephosphorylation by the nuclear isoform of T cell protein tyrosine phosphatase (TC45) in nucleus. Here we show that beta-arrestin1 directly interacts with STAT1 in nucleus after IFN-gamma treatment and accelerates STAT1 tyrosine dephosphorylation by recruiting TC45. Consequently, beta-arrestin1 negatively regulates STAT1 transcription activity as well as the IFN-gamma-induced gene transcription. Application of beta-arrestin1 siRNA significantly enhances IFN-gamma-induced antiviral response in vesicular stomatitis virus (VSV)-infected cells. Our results reveal that nuclear beta-arrestin1, acting as a scaffold for the dephosphorylation of STAT1, is an essential negative regulator of IFN-gamma signaling and participates in the IFN-gamma-induced cellular antiviral response. | lld:pubmed |
| pubmed-article:18775329 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18775329 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18775329 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18775329 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18775329 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18775329 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18775329 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:18775329 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18775329 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18775329 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18775329 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:18775329 | pubmed:issn | 1097-4164 | lld:pubmed |
| pubmed-article:18775329 | pubmed:author | pubmed-author:YehEE | lld:pubmed |
| pubmed-article:18775329 | pubmed:author | pubmed-author:CinaJJ | lld:pubmed |
| pubmed-article:18775329 | pubmed:author | pubmed-author:ZhangLiangL | lld:pubmed |
| pubmed-article:18775329 | pubmed:author | pubmed-author:HuangRuiminR | lld:pubmed |
| pubmed-article:18775329 | pubmed:author | pubmed-author:HuGengxiG | lld:pubmed |
| pubmed-article:18775329 | pubmed:author | pubmed-author:HuiLijianL | lld:pubmed |
| pubmed-article:18775329 | pubmed:author | pubmed-author:YangGuohuaG | lld:pubmed |
| pubmed-article:18775329 | pubmed:author | pubmed-author:HuZhonghuaZ | lld:pubmed |
| pubmed-article:18775329 | pubmed:author | pubmed-author:ChenYueleiY | lld:pubmed |
| pubmed-article:18775329 | pubmed:author | pubmed-author:ZhaiJianweiJ | lld:pubmed |
| pubmed-article:18775329 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:18775329 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:18775329 | pubmed:volume | 31 | lld:pubmed |
| pubmed-article:18775329 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18775329 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18775329 | pubmed:pagination | 695-707 | lld:pubmed |
| pubmed-article:18775329 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:18775329 | pubmed:meshHeading | pubmed-meshheading:18775329... | lld:pubmed |
| pubmed-article:18775329 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18775329 | pubmed:articleTitle | Nuclear beta-arrestin1 functions as a scaffold for the dephosphorylation of STAT1 and moderates the antiviral activity of IFN-gamma. | lld:pubmed |
| pubmed-article:18775329 | pubmed:affiliation | State Key Laboratory of Molecular Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China. | lld:pubmed |
| pubmed-article:18775329 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18775329 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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