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

Author

Listed:
  • 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)

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.

Suggested Citation

  • Ming-Juan Luo & Zhaolan Zhou & Keith Magni & Claudine Christoforides & Juri Rappsilber & Matthias Mann & Robin Reed, 2001. "Pre-mRNA splicing and mRNA export linked by direct interactions between UAP56 and Aly," Nature, Nature, vol. 413(6856), pages 644-647, October.
    • Handle: RePEc:nat:nature:v:413:y:2001:i:6856:d:10.1038_35098106
    DOI: 10.1038/35098106
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    Cited by:

    1. Ken-ichi Fujita & Misa Ito & Midori Irie & Kotaro Harada & Naoko Fujiwara & Yuya Ikeda & Hanae Yoshioka & Tomohiro Yamazaki & Masaki Kojima & Bunzo Mikami & Akila Mayeda & Seiji Masuda, 2024. "Structural differences between the closely related RNA helicases, UAP56 and URH49, fashion distinct functional apo-complexes," Nature Communications, Nature, vol. 15(1), pages 1-16, December.
    2. Ross A. Cordiner & Yuhui Dou & Rune Thomsen & Andrii Bugai & Sander Granneman & Torben Heick Jensen, 2023. "Temporal-iCLIP captures co-transcriptional RNA-protein interactions," Nature Communications, Nature, vol. 14(1), pages 1-16, December.

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