pubmed-article:16354698 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:16354698 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
pubmed-article:16354698 | lifeskim:mentions | umls-concept:C0040711 | lld:lifeskim |
pubmed-article:16354698 | lifeskim:mentions | umls-concept:C0035696 | lld:lifeskim |
pubmed-article:16354698 | lifeskim:mentions | umls-concept:C1823882 | lld:lifeskim |
pubmed-article:16354698 | lifeskim:mentions | umls-concept:C1705920 | lld:lifeskim |
pubmed-article:16354698 | lifeskim:mentions | umls-concept:C1515877 | lld:lifeskim |
pubmed-article:16354698 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
pubmed-article:16354698 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:16354698 | pubmed:dateCreated | 2005-12-15 | lld:pubmed |
pubmed-article:16354698 | pubmed:abstractText | YB-1 is a broad-specificity RNA-binding protein that is involved in regulation of mRNA transcription, splicing, translation, and stability. In both germinal and somatic cells, YB-1 and related proteins are major components of translationally inactive messenger ribonucleoprotein particles (mRNPs) and are mainly responsible for storage of mRNAs in a silent state. However, mechanisms regulating the repressor activity of YB-1 are not well understood. Here we demonstrate that association of YB-1 with the capped 5' terminus of the mRNA is regulated via phosphorylation by the serine/threonine protein kinase Akt. In contrast to its nonphosphorylated form, phosphorylated YB-1 fails to inhibit cap-dependent but not internal ribosome entry site-dependent translation of a reporter mRNA in vitro. We also show that similar to YB-1, Akt is associated with inactive mRNPs and that activated Akt may relieve translational repression of the YB-1-bound mRNAs. Using Affymetrix microarrays, we found that many of the YB-1-associated messages encode stress- and growth-related proteins, raising the intriguing possibility that Akt-mediated YB-1 phosphorylation could, in part, increase production of proteins regulating cell proliferation, oncogenic transformation, and stress response. | lld:pubmed |
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pubmed-article:16354698 | pubmed:language | eng | lld:pubmed |
pubmed-article:16354698 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16354698 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:16354698 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16354698 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16354698 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16354698 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16354698 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16354698 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16354698 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16354698 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:16354698 | pubmed:month | Jan | lld:pubmed |
pubmed-article:16354698 | pubmed:issn | 0270-7306 | lld:pubmed |
pubmed-article:16354698 | pubmed:author | pubmed-author:SonenbergNahu... | lld:pubmed |
pubmed-article:16354698 | pubmed:author | pubmed-author:SorensenPoul... | lld:pubmed |
pubmed-article:16354698 | pubmed:author | pubmed-author:OvchinnikovLe... | lld:pubmed |
pubmed-article:16354698 | pubmed:author | pubmed-author:TricheTimothy... | lld:pubmed |
pubmed-article:16354698 | pubmed:author | pubmed-author:BuckleyJonath... | lld:pubmed |
pubmed-article:16354698 | pubmed:author | pubmed-author:EvdokimovaVal... | lld:pubmed |
pubmed-article:16354698 | pubmed:author | pubmed-author:AnglesioMicha... | lld:pubmed |
pubmed-article:16354698 | pubmed:author | pubmed-author:SorokinAlexey... | lld:pubmed |
pubmed-article:16354698 | pubmed:author | pubmed-author:RuzanovPeterP | lld:pubmed |
pubmed-article:16354698 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:16354698 | pubmed:volume | 26 | lld:pubmed |
pubmed-article:16354698 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:16354698 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:16354698 | pubmed:pagination | 277-92 | lld:pubmed |
pubmed-article:16354698 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:16354698 | pubmed:year | 2006 | lld:pubmed |