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A cryptic RNA-binding domain mediates Syncrip recognition and exosomal partitioning of miRNA targets

Author

Listed:
  • Fruzsina Hobor

    (University College London, Darwin Building
    Faculty of Biological Sciences, University of Leeds)

  • Andre Dallmann

    (University College London, Darwin Building
    Humboldt Universität zu Berlin)

  • Neil J. Ball

    (The Francis Crick Institute)

  • Carla Cicchini

    (Sapienza University of Rome)

  • Cecilia Battistelli

    (Sapienza University of Rome)

  • Roksana W. Ogrodowicz

    (The Francis Crick Institute)

  • Evangelos Christodoulou

    (The Francis Crick Institute)

  • Stephen R. Martin

    (The Francis Crick Institute)

  • Alfredo Castello

    (University of Oxford)

  • Marco Tripodi

    (Sapienza University of Rome)

  • Ian A. Taylor

    (The Francis Crick Institute)

  • Andres Ramos

    (University College London, Darwin Building)

Abstract

Exosomal miRNA transfer is a mechanism for cell–cell communication that is important in the immune response, in the functioning of the nervous system and in cancer. Syncrip/hnRNPQ is a highly conserved RNA-binding protein that mediates the exosomal partition of a set of miRNAs. Here, we report that Syncrip’s amino-terminal domain, which was previously thought to mediate protein–protein interactions, is a cryptic, conserved and sequence-specific RNA-binding domain, designated NURR (N-terminal unit for RNA recognition). The NURR domain mediates the specific recognition of a short hEXO sequence defining Syncrip exosomal miRNA targets, and is coupled by a non-canonical structural element to Syncrip’s RRM domains to achieve high-affinity miRNA binding. As a consequence, Syncrip-mediated selection of the target miRNAs implies both recognition of the hEXO sequence by the NURR domain and binding of the RRM domains 5′ to this sequence. This structural arrangement enables Syncrip-mediated selection of miRNAs with different seed sequences.

Suggested Citation

  • Fruzsina Hobor & Andre Dallmann & Neil J. Ball & Carla Cicchini & Cecilia Battistelli & Roksana W. Ogrodowicz & Evangelos Christodoulou & Stephen R. Martin & Alfredo Castello & Marco Tripodi & Ian A. , 2018. "A cryptic RNA-binding domain mediates Syncrip recognition and exosomal partitioning of miRNA targets," Nature Communications, Nature, vol. 9(1), pages 1-16, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-03182-3
    DOI: 10.1038/s41467-018-03182-3
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    Cited by:

    1. Malgorzata M. Duszczyk & Harry Wischnewski & Tamara Kazeeva & Rajika Arora & Fionna E. Loughlin & Christine Schroetter & Ugo Pradère & Jonathan Hall & Constance Ciaudo & Frédéric H.-T. Allain, 2022. "The solution structure of Dead End bound to AU-rich RNA reveals an unusual mode of tandem RRM-RNA recognition required for mRNA regulation," Nature Communications, Nature, vol. 13(1), pages 1-17, December.

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