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pubmed-article:16354698pubmed:abstractTextYB-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:16354698pubmed:authorpubmed-author:SonenbergNahu...lld:pubmed
pubmed-article:16354698pubmed:authorpubmed-author:SorensenPoul...lld:pubmed
pubmed-article:16354698pubmed:authorpubmed-author:OvchinnikovLe...lld:pubmed
pubmed-article:16354698pubmed:authorpubmed-author:TricheTimothy...lld:pubmed
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pubmed-article:16354698pubmed:authorpubmed-author:EvdokimovaVal...lld:pubmed
pubmed-article:16354698pubmed:authorpubmed-author:AnglesioMicha...lld:pubmed
pubmed-article:16354698pubmed:authorpubmed-author:SorokinAlexey...lld:pubmed
pubmed-article:16354698pubmed:authorpubmed-author:RuzanovPeterPlld:pubmed
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pubmed-article:16354698pubmed:dateRevised2009-11-19lld:pubmed
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