Journal
SCIENCE
Volume 293, Issue 5536, Pages 1836-1839Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1062786
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- NCI NIH HHS [CA 16038] Funding Source: Medline
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In mammalian cells, splice junctions play a dual rote 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.
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