Abstract
In mammalian cells, splice junctions play a dual role in mRNA quality control: They mediate selective nuclear export of mature mRNA and they serve as a mark for mRNA surveillance, which subjects aberrant mRNAs with premature termination codons to nonsense-mediated decay (NMD). Here, we demonstrate that the protein RNPS1, a component of the postsplicing complex that is deposited 5' to exon-exon junctions, interacts with the evolutionarily conserved human Upf complex, a central component of NMD. Significantly, RNPS1 triggers NMD when tethered to the 3' untranslated region of beta-globin mRNA, demonstrating its role as a subunit of the postsplicing complex directly involved in mRNA surveillance.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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3' Untranslated Regions / genetics
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3' Untranslated Regions / metabolism
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Animals
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Cell Line
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DNA-Binding Proteins / genetics
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DNA-Binding Proteins / metabolism*
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Exons / genetics*
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Fungal Proteins / metabolism
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Globins / genetics
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HeLa Cells
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Humans
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Macromolecular Substances
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Mice
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Models, Biological
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Precipitin Tests
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Protein Binding
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RNA Helicases / metabolism
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RNA Splicing
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RNA, Messenger / genetics
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RNA, Messenger / metabolism*
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RNA-Binding Proteins / genetics
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RNA-Binding Proteins / metabolism*
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Recombinant Fusion Proteins / metabolism
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Ribonucleoproteins*
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Saccharomyces cerevisiae Proteins
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Trans-Activators
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Transfection
Substances
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3' Untranslated Regions
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DNA-Binding Proteins
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Fungal Proteins
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Macromolecular Substances
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RNA, Messenger
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RNA-Binding Proteins
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RNPS1 protein, human
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Recombinant Fusion Proteins
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Rent1 protein, mouse
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Ribonucleoproteins
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Rnps1 protein, mouse
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Saccharomyces cerevisiae Proteins
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Trans-Activators
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UPF3 protein, S cerevisiae
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Globins
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RNA Helicases
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UPF1 protein, human