Pre-mRNA splicing and mRNA export linked by direct interactions between UAP56 and Aly

Ming-Juan Luo, Zhaolan Zhou, Keith Magni, Claudine Christoforides, Juri Rappsilber, Matthias Mann and Robin Reed ()
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Ming-Juan Luo: Harvard Medical School
Zhaolan Zhou: Harvard Medical School
Keith Magni: Harvard Medical School
Claudine Christoforides: Harvard Medical School
Juri Rappsilber: Protein Interaction Laboratory in the Center of Experimental Bioinformatics, University of Southern Denmark, Campusvej 55
Matthias Mann: Protein Interaction Laboratory in the Center of Experimental Bioinformatics, University of Southern Denmark, Campusvej 55
Robin Reed: Harvard Medical School

Nature, 2001, vol. 413, issue 6856, 644-647

Abstract: Abstract Recent studies indicate that splicing of pre-messenger RNA and export of mRNA are normally coupled in vivo1,2,3,4,5,6. During splicing, the conserved mRNA export factor Aly is recruited to the spliced mRNA–protein complex (mRNP), which targets the mRNA for export. At present, it is not known how Aly is recruited to the spliced mRNP. Here we show that the conserved DEAD-box helicase UAP56, which functions during spliceosome assembly7,8,9,10, interacts directly and highly specifically with Aly. Moreover, UAP56 is present together with Aly in the spliced mRNP. Significantly, excess UAP56 is a potent dominant negative inhibitor of mRNA export. Excess UAP56 also inhibits the recruitment of Aly to the spliced mRNP. Furthermore, a mutation in Aly that blocks its interaction with UAP56 prevents recruitment of Aly to the spliced mRNP. These data suggest that the splicing factor UAP56 functions in coupling the splicing and export machineries by recruiting Aly to the spliced mRNP.

Date: 2001
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DOI: 10.1038/35098106

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