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A CAF40-binding motif facilitates recruitment of the CCR4-NOT complex to mRNAs targeted by Drosophila Roquin

Author

Listed:
  • Annamaria Sgromo

    (Max Planck Institute for Developmental Biology)

  • Tobias Raisch

    (Max Planck Institute for Developmental Biology)

  • Praveen Bawankar

    (Max Planck Institute for Developmental Biology)

  • Dipankar Bhandari

    (Max Planck Institute for Developmental Biology)

  • Ying Chen

    (Max Planck Institute for Developmental Biology)

  • Duygu Kuzuoğlu-Öztürk

    (Max Planck Institute for Developmental Biology)

  • Oliver Weichenrieder

    (Max Planck Institute for Developmental Biology)

  • Elisa Izaurralde

    (Max Planck Institute for Developmental Biology)

Abstract

Human (Hs) Roquin1 and Roquin2 are RNA-binding proteins that promote mRNA target degradation through the recruitment of the CCR4-NOT deadenylase complex and are implicated in the prevention of autoimmunity. Roquin1 recruits CCR4-NOT via a C-terminal region that is not conserved in Roquin2 or in invertebrate Roquin. Here we show that Roquin2 and Drosophila melanogaster (Dm) Roquin also interact with the CCR4-NOT complex through their C-terminal regions. The C-terminal region of Dm Roquin contains multiple motifs that mediate CCR4-NOT binding. One motif binds to the CAF40 subunit of the CCR4-NOT complex. The crystal structure of the Dm Roquin CAF40-binding motif (CBM) bound to CAF40 reveals that the CBM adopts an α-helical conformation upon binding to a conserved surface of CAF40. Thus, despite the lack of sequence conservation, the C-terminal regions of Roquin proteins act as an effector domain that represses the expression of mRNA targets via recruitment of the CCR4-NOT complex.

Suggested Citation

  • Annamaria Sgromo & Tobias Raisch & Praveen Bawankar & Dipankar Bhandari & Ying Chen & Duygu Kuzuoğlu-Öztürk & Oliver Weichenrieder & Elisa Izaurralde, 2017. "A CAF40-binding motif facilitates recruitment of the CCR4-NOT complex to mRNAs targeted by Drosophila Roquin," Nature Communications, Nature, vol. 8(1), pages 1-16, April.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms14307
    DOI: 10.1038/ncomms14307
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    Cited by:

    1. Harpreet Kaur Salgania & Jutta Metz & Mandy Jeske, 2024. "ReLo is a simple and rapid colocalization assay to identify and characterize direct protein–protein interactions," Nature Communications, Nature, vol. 15(1), pages 1-12, December.
    2. Kriti Shah & Shiyang He & David J. Turner & Joshua Corbo & Khadija Rebbani & Daniel Dominguez & Joseph M. Bateman & Sihem Cheloufi & Cátia Igreja & Eugene Valkov & Jernej Murn, 2024. "Regulation by the RNA-binding protein Unkempt at its effector interface," Nature Communications, Nature, vol. 15(1), pages 1-18, December.
    3. Fabian Poetz & Joshua Corbo & Yevgen Levdansky & Alexander Spiegelhalter & Doris Lindner & Vera Magg & Svetlana Lebedeva & Jörg Schweiggert & Johanna Schott & Eugene Valkov & Georg Stoecklin, 2021. "RNF219 attenuates global mRNA decay through inhibition of CCR4-NOT complex-mediated deadenylation," Nature Communications, Nature, vol. 12(1), pages 1-19, December.

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