pubmed-article:20484576 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:20484576 | lifeskim:mentions | umls-concept:C1179132 | lld:lifeskim |
pubmed-article:20484576 | lifeskim:mentions | umls-concept:C1579259 | lld:lifeskim |
pubmed-article:20484576 | lifeskim:mentions | umls-concept:C1823478 | lld:lifeskim |
pubmed-article:20484576 | lifeskim:mentions | umls-concept:C1523116 | lld:lifeskim |
pubmed-article:20484576 | lifeskim:mentions | umls-concept:C0336821 | lld:lifeskim |
pubmed-article:20484576 | pubmed:issue | 14 | lld:pubmed |
pubmed-article:20484576 | pubmed:dateCreated | 2010-7-14 | lld:pubmed |
pubmed-article:20484576 | pubmed:abstractText | TANK/I-TRAF is a TRAF-binding protein that negatively regulates NF-kappaB activation. The underlying mechanism of this activity remains unclear. Here we show that TANK directly interacts with PLK1, a conserved cell cycle-regulated kinase. PLK1 inhibits NF-kappaB transcriptional activation induced by TNF-alpha, IL-1beta, or several activators, but not by nuclear transcription factor p65. PLK1 expression reduces the DNA-binding activity of NF-kappaB induced by TNF-alpha. Moreover, endogenous activation of PLK1 reduces the TNF-induced phosphorylation of endogenous IkappaBalpha. PLK1 is bound to NEMO (IKKgamma) through TANK to form a ternary complex in vivo. We describe a new regulatory mechanism for PLK1: PLK1 negatively regulates TNF-induced IKK activation by inhibiting the ubiquitination of NEMO. These findings reveal that the scaffold protein TANK recruits PLK1 to negatively regulate NF-kappaB activation and provide direct evidence that PLK1 is required for the repression function of TANK. | lld:pubmed |
pubmed-article:20484576 | pubmed:language | eng | lld:pubmed |
pubmed-article:20484576 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20484576 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:20484576 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20484576 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20484576 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20484576 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20484576 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20484576 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20484576 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20484576 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20484576 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20484576 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20484576 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20484576 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20484576 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20484576 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:20484576 | pubmed:month | Jul | lld:pubmed |
pubmed-article:20484576 | pubmed:issn | 1939-4586 | lld:pubmed |
pubmed-article:20484576 | pubmed:author | pubmed-author:HuntM FMF | lld:pubmed |
pubmed-article:20484576 | pubmed:author | pubmed-author:WangJianJ | lld:pubmed |
pubmed-article:20484576 | pubmed:author | pubmed-author:YangXiaomingX | lld:pubmed |
pubmed-article:20484576 | pubmed:author | pubmed-author:HeFuchuF | lld:pubmed |
pubmed-article:20484576 | pubmed:author | pubmed-author:ZhangYingY | lld:pubmed |
pubmed-article:20484576 | pubmed:author | pubmed-author:FUSTBB | lld:pubmed |
pubmed-article:20484576 | pubmed:author | pubmed-author:WangXiaohuiX | lld:pubmed |
pubmed-article:20484576 | pubmed:author | pubmed-author:YuanYanzhiY | lld:pubmed |
pubmed-article:20484576 | pubmed:author | pubmed-author:JinChaozhiC | lld:pubmed |
pubmed-article:20484576 | pubmed:author | pubmed-author:ZhangWanqiaoW | lld:pubmed |
pubmed-article:20484576 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:20484576 | pubmed:day | 15 | lld:pubmed |
pubmed-article:20484576 | pubmed:volume | 21 | lld:pubmed |
pubmed-article:20484576 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:20484576 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:20484576 | pubmed:pagination | 2500-13 | lld:pubmed |
pubmed-article:20484576 | pubmed:dateRevised | 2011-11-2 | lld:pubmed |
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pubmed-article:20484576 | pubmed:year | 2010 | lld:pubmed |
pubmed-article:20484576 | pubmed:articleTitle | The scaffold protein TANK/I-TRAF inhibits NF-kappaB activation by recruiting polo-like kinase 1. | lld:pubmed |
pubmed-article:20484576 | pubmed:affiliation | State Key Laboratory of Proteomics, Beijing Proteome Research Center, Beijing Institute of Radiation Medicine, Beijing 102206, China. | lld:pubmed |
pubmed-article:20484576 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:20484576 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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