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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6976
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pubmed:dateCreated |
2004-2-19
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pubmed:abstractText |
The specification of both the germ line and abdomen in Drosophila depends on the localization of oskar messenger RNA to the posterior of the oocyte. This localization requires several trans-acting factors, including Barentsz and the Mago-Y14 heterodimer, which assemble with oskar mRNA into ribonucleoprotein particles (RNPs) and localize with it at the posterior pole. Although Barentsz localization in the germ line depends on Mago-Y14, no direct interaction between these proteins has been detected. Here, we demonstrate that the translation initiation factor eIF4AIII interacts with Barentsz and is a component of the oskar messenger RNP localization complex. Moreover, eIF4AIII interacts with Mago-Y14 and thus provides a molecular link between Barentsz and the heterodimer. The mammalian Mago (also known as Magoh)-Y14 heterodimer is a component of the exon junction complex. The exon junction complex is deposited on spliced mRNAs and functions in nonsense-mediated mRNA decay (NMD), a surveillance mechanism that degrades mRNAs with premature translation-termination codons. We show that both Barentsz and eIF4AIII are essential for NMD in human cells. Thus, we have identified eIF4AIII and Barentsz as components of a conserved protein complex that is essential for mRNA localization in flies and NMD in mammals.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Barentsz protein, Drosophila,
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Eukaryotic Initiation Factor-4A,
http://linkedlifedata.com/resource/pubmed/chemical/MAGOH protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Mago protein, Drosophila,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RBM8A protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/messenger ribonucleoprotein,
http://linkedlifedata.com/resource/pubmed/chemical/oskar protein, Drosophila
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
1476-4687
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
19
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pubmed:volume |
427
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
753-7
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:14973490-Active Transport, Cell Nucleus,
pubmed-meshheading:14973490-Animals,
pubmed-meshheading:14973490-Dimerization,
pubmed-meshheading:14973490-Drosophila Proteins,
pubmed-meshheading:14973490-Drosophila melanogaster,
pubmed-meshheading:14973490-Eukaryotic Initiation Factor-4A,
pubmed-meshheading:14973490-Exons,
pubmed-meshheading:14973490-HeLa Cells,
pubmed-meshheading:14973490-Humans,
pubmed-meshheading:14973490-Nuclear Proteins,
pubmed-meshheading:14973490-Protein Binding,
pubmed-meshheading:14973490-Protein Biosynthesis,
pubmed-meshheading:14973490-RNA, Messenger,
pubmed-meshheading:14973490-RNA Splicing,
pubmed-meshheading:14973490-RNA Stability,
pubmed-meshheading:14973490-RNA Transport,
pubmed-meshheading:14973490-RNA-Binding Proteins,
pubmed-meshheading:14973490-Ribonucleoproteins
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pubmed:year |
2004
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pubmed:articleTitle |
An eIF4AIII-containing complex required for mRNA localization and nonsense-mediated mRNA decay.
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pubmed:affiliation |
Wellcome Trust/Cancer Research UK Institute and Department of Genetics, University of Cambridge, Tennis Court Road, Cambridge CB2 1QR, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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