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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
41
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pubmed:dateCreated |
2005-10-10
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pubmed:abstractText |
The multicomponent exon junction complex (EJC) is deposited on the spliced mRNA during pre-mRNA splicing and is implicated in several post-splicing events, including mRNA export, nonsense-mediated mRNA decay (NMD), and translation control. This report is the first to identify potential post-translational modifications of the EJC core component Y14. We demonstrate that Y14 is phosphorylated at its repeated arginine/serine (RS) dipeptides, likely by SR protein-specific kinases. Phosphorylation of Y14 abolished its interaction with EJC components as well as factors that function downstream of the EJC. A non-phosphorylatable Y14 mutant was equivalent to the wild-type protein with respect to its association with spliced mRNA and its ability in NMD activation, but the mutant sequestered EJC and NMD factors on ribosome-containing mRNA ribonucleoproteins (mRNPs). We therefore hypothesize that phosphorylation of Y14 occurs upon completion of mRNA surveillance, leading to dissociation of Y14 from ribosome-containing mRNPs. Moreover, we found that Y14 is possibly methylated at multiple arginine residues in the carboxyl-terminal domain and that methylation of Y14 was antagonized by phosphorylation of RS dipeptides. This study reveals antagonistic post-translational modifications of Y14 that may be involved in the remodeling of Y14-containing mRNPs.
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:volume |
280
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
34507-12
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:16100109-Amino Acid Sequence,
pubmed-meshheading:16100109-Animals,
pubmed-meshheading:16100109-Arginine,
pubmed-meshheading:16100109-Exons,
pubmed-meshheading:16100109-Glutathione Transferase,
pubmed-meshheading:16100109-HeLa Cells,
pubmed-meshheading:16100109-Humans,
pubmed-meshheading:16100109-Introns,
pubmed-meshheading:16100109-Methylation,
pubmed-meshheading:16100109-Models, Biological,
pubmed-meshheading:16100109-Models, Genetic,
pubmed-meshheading:16100109-Molecular Sequence Data,
pubmed-meshheading:16100109-Mutation,
pubmed-meshheading:16100109-Oocytes,
pubmed-meshheading:16100109-Peptides,
pubmed-meshheading:16100109-Phosphorylation,
pubmed-meshheading:16100109-Plasmids,
pubmed-meshheading:16100109-Protein Binding,
pubmed-meshheading:16100109-Protein Structure, Tertiary,
pubmed-meshheading:16100109-RNA,
pubmed-meshheading:16100109-RNA, Messenger,
pubmed-meshheading:16100109-RNA Splicing,
pubmed-meshheading:16100109-RNA-Binding Proteins,
pubmed-meshheading:16100109-Recombinant Proteins,
pubmed-meshheading:16100109-Transfection,
pubmed-meshheading:16100109-Xenopus laevis
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pubmed:year |
2005
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pubmed:articleTitle |
Phosphorylation of Y14 modulates its interaction with proteins involved in mRNA metabolism and influences its methylation.
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pubmed:affiliation |
Institute of Biomedical Sciences, Academia Sinica, Taipei 11529, Taiwan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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