| pubmed-article:12920522 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12920522 | lifeskim:mentions | umls-concept:C1167128 | lld:lifeskim |
| pubmed-article:12920522 | lifeskim:mentions | umls-concept:C0079904 | lld:lifeskim |
| pubmed-article:12920522 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:12920522 | lifeskim:mentions | umls-concept:C0001038 | lld:lifeskim |
| pubmed-article:12920522 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:12920522 | lifeskim:mentions | umls-concept:C0205460 | lld:lifeskim |
| pubmed-article:12920522 | pubmed:issue | 9 | lld:pubmed |
| pubmed-article:12920522 | pubmed:dateCreated | 2003-9-23 | lld:pubmed |
| pubmed-article:12920522 | pubmed:abstractText | Although the proximal cytoplasmic signaling events that control the activation of the NF-kappaB transcription factor are understood in considerable detail, the subsequent intranuclear events that regulate the strength and duration of the NF-kappaB-mediated transcriptional response remain poorly defined. Recent studies have revealed that NF-kappaB is subject to reversible acetylation and that this posttranslational modification functions as an intranuclear molecular switch to control NF-kappaB action. In this review, we summarize this new and fascinating mechanism through which the pleiotropic effects of NF-kappaB are regulated within the cells. NF-kappaB is a heterodimer composed of p50 and RelA subunits. Both subunits are acetylated at multiple lysine residues with the p300/CBP acetyltransferases playing a major role in this process in vivo. Further, the acetylation of different lysines regulates different functions of NF-kappaB, including transcriptional activation, DNA binding affinity, IkappaBalpha assembly, and subcellular localization. Acetylated forms RelA are subject to deacetylation by histone deacetylase 3 (HDAC3). This selective action of HDAC3 promotes IkappaBalpha binding and rapid CRM1-dependent nuclear export of the deacetylated NF-kappaB complex, which terminates the NF-kappaB response and replenishes the cytoplasmic pool of latent NF-kappaB/IkappaBalpha complexes. This readies the cell for the next NF-kappaB-inducing stimulus. Thus, reversible acetylation of RelA serves as an important intranuclear regulatory mechanism that further provides for dynamic control of NF-kappaB action. | lld:pubmed |
| pubmed-article:12920522 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:12920522 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12920522 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12920522 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:12920522 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12920522 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:12920522 | pubmed:issn | 0946-2716 | lld:pubmed |
| pubmed-article:12920522 | pubmed:author | pubmed-author:GreeneWarner... | lld:pubmed |
| pubmed-article:12920522 | pubmed:author | pubmed-author:ChenLin-FengL... | lld:pubmed |
| pubmed-article:12920522 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12920522 | pubmed:volume | 81 | lld:pubmed |
| pubmed-article:12920522 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12920522 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12920522 | pubmed:pagination | 549-57 | lld:pubmed |
| pubmed-article:12920522 | pubmed:dateRevised | 2011-7-8 | lld:pubmed |
| pubmed-article:12920522 | pubmed:meshHeading | pubmed-meshheading:12920522... | lld:pubmed |
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| pubmed-article:12920522 | pubmed:meshHeading | pubmed-meshheading:12920522... | lld:pubmed |
| pubmed-article:12920522 | pubmed:meshHeading | pubmed-meshheading:12920522... | lld:pubmed |
| pubmed-article:12920522 | pubmed:meshHeading | pubmed-meshheading:12920522... | lld:pubmed |
| pubmed-article:12920522 | pubmed:meshHeading | pubmed-meshheading:12920522... | lld:pubmed |
| pubmed-article:12920522 | pubmed:meshHeading | pubmed-meshheading:12920522... | lld:pubmed |
| pubmed-article:12920522 | pubmed:meshHeading | pubmed-meshheading:12920522... | lld:pubmed |
| pubmed-article:12920522 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12920522 | pubmed:articleTitle | Regulation of distinct biological activities of the NF-kappaB transcription factor complex by acetylation. | lld:pubmed |
| pubmed-article:12920522 | pubmed:affiliation | Gladstone Institute of Virology and Immunology, University of California, P.O. Box 419100, San Francisco, CA 94141-9100, USA. | lld:pubmed |
| pubmed-article:12920522 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12920522 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:12920522 | pubmed:publicationType | Review | lld:pubmed |
| pubmed-article:12920522 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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