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Role of the nonsense-mediated decay factor hUpf3 in the splicing-dependent exon-exon junction complex

Cited 241 time in Web of Science Cited 250 time in Scopus
Authors

Kim, V. Narry; Kataoka, Naoyuki; Dreyfuss, Gideon

Issue Date
2001-09
Publisher
American Association for the Advancement of Science
Citation
Science, Vol.293 No.5536, pp.1832-1836
Abstract
Nonsense-mediated messenger RNA (mRNA) decay, or NMD, is a critical process of selective degradation of mRNAs that contain premature stop codons. NMD depends on both pre-mRNA splicing and translation, and it requires recognition of the position of stop codons relative to exon-exon junctions. A key factor in NMD is hUpf3, a mostly nuclear protein that shuttles between the nucleus and cytoplasm and interacts specifically with spliced mRNAs. We found that hUpf3 interacts with Y14, a component of post-splicing mRNA-protein (mRNP) complexes, and that hUpf3 is enriched in Y14-containing mRNP complexes. The mRNA export factors Aly/REF and TAP are also associated with nuclear hUpf3, indicating that hUpf3 is in mRNP complexes that are poised for nuclear export. Like Y14 and Aly/REF, hUpf3 binds to spliced mRNAs specifically (similar to 20 nucleotides) upstream of exon-exon junctions. The splicing-dependent binding of hUpf3 to mRNAs before export, as part of the complex that assembles near exon-exon junctions, allows it to serve as a link between splicing and NMD in the cytoplasm.
ISSN
0036-8075
URI
https://hdl.handle.net/10371/171903
DOI
https://doi.org/10.1126/science.1062829
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  • College of Natural Sciences
  • School of Biological Sciences
Research Area Molecular Biology & Genetics

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