| pubmed-article:12819194 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12819194 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:12819194 | lifeskim:mentions | umls-concept:C0035544 | lld:lifeskim |
| pubmed-article:12819194 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:12819194 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
| pubmed-article:12819194 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:12819194 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:12819194 | lifeskim:mentions | umls-concept:C0013879 | lld:lifeskim |
| pubmed-article:12819194 | lifeskim:mentions | umls-concept:C0443172 | lld:lifeskim |
| pubmed-article:12819194 | pubmed:issue | 35 | lld:pubmed |
| pubmed-article:12819194 | pubmed:dateCreated | 2003-8-25 | lld:pubmed |
| pubmed-article:12819194 | pubmed:abstractText | Messenger RNA turnover directed by A + U-rich elements (AREs) involves selected ARE-binding proteins. Whereas several signaling systems may modulate ARE-directed mRNA decay and/or post-translationally modify specific trans-acting factors, it is unclear how these mechanisms are linked. In THP-1 monocytic leukemia cells, phorbol ester-induced stabilization of some mRNAs containing AREs was accompanied by dephosphorylation of Ser83 and Ser87 of polysome-associated p40AUF1. Here, we report that phosphorylation of p40AUF1 influences its ARE-binding affinity as well as the RNA conformational dynamics and global structure of the p40AUF1-ARE ribonucleoprotein complex. Most notably, association of unphosphorylated p40AUF1 induces a condensed RNA conformation upon ARE substrates. By contrast, phosphorylation of p40AUF1 at Ser83 and Ser87 inhibits this RNA structural transition. These data indicate that selective AUF1 phosphorylation may regulate ARE-directed mRNA turnover by remodeling local RNA structures, thus potentially altering the presentation of RNA and/or protein determinants involved in subsequent trans-factor recruitment. | lld:pubmed |
| pubmed-article:12819194 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12819194 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12819194 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12819194 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12819194 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:12819194 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:12819194 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12819194 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12819194 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:12819194 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:12819194 | pubmed:author | pubmed-author:BrewerGaryG | lld:pubmed |
| pubmed-article:12819194 | pubmed:author | pubmed-author:WilsonGerald... | lld:pubmed |
| pubmed-article:12819194 | pubmed:author | pubmed-author:SandyCharlesC | lld:pubmed |
| pubmed-article:12819194 | pubmed:author | pubmed-author:LuJieboJ | lld:pubmed |
| pubmed-article:12819194 | pubmed:author | pubmed-author:SutphenKristi... | lld:pubmed |
| pubmed-article:12819194 | pubmed:author | pubmed-author:SuarezYveliss... | lld:pubmed |
| pubmed-article:12819194 | pubmed:author | pubmed-author:SinhaSmritaS | lld:pubmed |
| pubmed-article:12819194 | pubmed:author | pubmed-author:BrewerBrandyB | lld:pubmed |
| pubmed-article:12819194 | pubmed:author | pubmed-author:Villanueva-Fe... | lld:pubmed |
| pubmed-article:12819194 | pubmed:author | pubmed-author:YslaRiza MRM | lld:pubmed |
| pubmed-article:12819194 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12819194 | pubmed:day | 29 | lld:pubmed |
| pubmed-article:12819194 | pubmed:volume | 278 | lld:pubmed |
| pubmed-article:12819194 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12819194 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12819194 | pubmed:pagination | 33039-48 | lld:pubmed |
| pubmed-article:12819194 | pubmed:dateRevised | 2011-11-2 | lld:pubmed |
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| pubmed-article:12819194 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12819194 | pubmed:articleTitle | Phosphorylation of p40AUF1 regulates binding to A + U-rich mRNA-destabilizing elements and protein-induced changes in ribonucleoprotein structure. | lld:pubmed |
| pubmed-article:12819194 | pubmed:affiliation | Department of Biochemistry and Molecular Biology and Center for Fluorescence Spectroscopy, University of Maryland School of Medicine, Baltimore, Maryland 21201, USA. gwils001@umaryland.edu | lld:pubmed |
| pubmed-article:12819194 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12819194 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:12819194 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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