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Structures of Teneurin adhesion receptors reveal an ancient fold for cell-cell interaction

Author

Listed:
  • Verity A. Jackson

    (Oxford University)

  • Dimphna H. Meijer

    (Utrecht University)

  • Maria Carrasquero

    (Oxford University)

  • Laura S. Bezouwen

    (Utrecht University
    Utrecht University)

  • Edward D. Lowe

    (Oxford University)

  • Colin Kleanthous

    (Oxford University)

  • Bert J. C. Janssen

    (Utrecht University)

  • Elena Seiradake

    (Oxford University)

Abstract

Teneurins are ancient cell–cell adhesion receptors that are vital for brain development and synapse organisation. They originated in early metazoan evolution through a horizontal gene transfer event when a bacterial YD-repeat toxin fused to a eukaryotic receptor. We present X-ray crystallography and cryo-EM structures of two Teneurins, revealing a ~200 kDa extracellular super-fold in which eight sub-domains form an intricate structure centred on a spiralling YD-repeat shell. An alternatively spliced loop, which is implicated in homophilic Teneurin interaction and specificity, is exposed and thus poised for interaction. The N-terminal side of the shell is ‘plugged’ via a fibronectin-plug domain combination, which defines a new class of YD proteins. Unexpectedly, we find that these proteins are widespread amongst modern bacteria, suggesting early metazoan receptor evolution from a distinct class of proteins, which today includes both bacterial proteins and eukaryotic Teneurins.

Suggested Citation

  • Verity A. Jackson & Dimphna H. Meijer & Maria Carrasquero & Laura S. Bezouwen & Edward D. Lowe & Colin Kleanthous & Bert J. C. Janssen & Elena Seiradake, 2018. "Structures of Teneurin adhesion receptors reveal an ancient fold for cell-cell interaction," Nature Communications, Nature, vol. 9(1), pages 1-9, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-03460-0
    DOI: 10.1038/s41467-018-03460-0
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    Cited by:

    1. Amaia González-Magaña & Igor Tascón & Jon Altuna-Alvarez & María Queralt-Martín & Jake Colautti & Carmen Velázquez & Maialen Zabala & Jessica Rojas-Palomino & Marité Cárdenas & Antonio Alcaraz & John , 2023. "Structural and functional insights into the delivery of a bacterial Rhs pore-forming toxin to the membrane," Nature Communications, Nature, vol. 14(1), pages 1-16, December.
    2. Brooke K. Hayes & Marina Harper & Hariprasad Venugopal & Jessica M. Lewis & Amy Wright & Han-Chung Lee & Joel R. Steele & David L. Steer & Ralf B. Schittenhelm & John D. Boyce & Sheena McGowan, 2024. "Structure of a Rhs effector clade domain provides mechanistic insights into type VI secretion system toxin delivery," Nature Communications, Nature, vol. 15(1), pages 1-15, December.
    3. Dukas Jurėnas & Leonardo Talachia Rosa & Martial Rey & Julia Chamot-Rooke & Rémi Fronzes & Eric Cascales, 2021. "Mounting, structure and autocleavage of a type VI secretion-associated Rhs polymorphic toxin," Nature Communications, Nature, vol. 12(1), pages 1-11, December.
    4. Xuchen Zhang & Pei-Yi Lin & Kif Liakath-Ali & Thomas C. Südhof, 2022. "Teneurins assemble into presynaptic nanoclusters that promote synapse formation via postsynaptic non-teneurin ligands," Nature Communications, Nature, vol. 13(1), pages 1-18, December.
    5. Christos Gogou & J. Wouter Beugelink & Cátia P. Frias & Leanid Kresik & Natalia Jaroszynska & Uwe Drescher & Bert J. C. Janssen & Robert Hindges & Dimphna H. Meijer, 2024. "Alternative splicing controls teneurin-3 compact dimer formation for neuronal recognition," Nature Communications, Nature, vol. 15(1), pages 1-15, December.
    6. Shiheng Liu & Xian Xia & Eric Calvo & Z. Hong Zhou, 2023. "Native structure of mosquito salivary protein uncovers domains relevant to pathogen transmission," Nature Communications, Nature, vol. 14(1), pages 1-12, December.

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