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Magoh, a human homolog of Drosophila mago nashi protein, is a component of the splicing-dependent exon-exon junction complex

Cited 161 time in Web of Science Cited 166 time in Scopus
Authors
Kataoka, Naoyuki; Diem, Michael D.; Kim, V. Narry; Yong, Jeongsik; Dreyfuss, Gideon
Issue Date
2001-11
Citation
EMBO Journal, Vol.20 No.22, pp.6424-6433
Keywords
exon-exon junction complexmagohmago nashisplicingY14
Abstract
The RNA-binding protein Y14 binds preferentially to mRNAs produced by splicing and is a component of a multiprotein complex that assembles similar to 20 nucleotides upstream of exon-exon junctions. This complex probably has important functions in post-splicing events including nuclear export and nonsense-mediated decay of mRNA. We show that Y14 binds to two previously reported components, Aly/REF and RNPS1, and to the mRNA export factor TAP. Moreover, we identified magoh, a human homolog of the Drosophila mago nashi gene product, as a novel component of the complex. Magoh binds avidly and directly to Y14 and TAP, but not to other known components of the complex, and is found in Y14-containing mRNPs in vivo. Importantly, magoh also binds to mRNAs produced by splicing upstream (similar to 20 nucleotides) of exon-exon junctions and its binding to mRNA persists after export. These experiments thus reveal specific protein-protein interactions among the proteins of the splicing-dependent mRNP complex and suggest an important role for the highly evolutionarily conserved magoh protein in this complex.
ISSN
0261-4189
URI
https://hdl.handle.net/10371/171884
DOI
https://doi.org/10.1093/emboj/20.22.6424
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College of Natural Sciences (자연과학대학)Dept. of Biological Sciences (생명과학부)Journal Papers (저널논문_생명과학부)
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