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Structural insights into the contactin 1 – neurofascin 155 adhesion complex

Author

Listed:
  • Lucas M. P. Chataigner

    (Utrecht University)

  • Christos Gogou

    (Delft University of Technology)

  • Maurits A. Boer

    (Utrecht University
    Netherlands Proteomics Center)

  • Cátia P. Frias

    (Delft University of Technology)

  • Dominique M. E. Thies-Weesie

    (Utrecht University)

  • Joke C. M. Granneman

    (Utrecht University)

  • Albert J. R. Heck

    (Utrecht University
    Netherlands Proteomics Center)

  • Dimphna H. Meijer

    (Delft University of Technology)

  • Bert J. C. Janssen

    (Utrecht University)

Abstract

Cell-surface expressed contactin 1 and neurofascin 155 control wiring of the nervous system and interact across cells to form and maintain paranodal myelin-axon junctions. The molecular mechanism of contactin 1 – neurofascin 155 adhesion complex formation is unresolved. Crystallographic structures of complexed and individual contactin 1 and neurofascin 155 binding regions presented here, provide a rich picture of how competing and complementary interfaces, post-translational glycosylation, splice differences and structural plasticity enable formation of diverse adhesion sites. Structural, biophysical, and cell-clustering analysis reveal how conserved Ig1-2 interfaces form competing heterophilic contactin 1 – neurofascin 155 and homophilic neurofascin 155 complexes whereas contactin 1 forms low-affinity clusters through interfaces on Ig3-6. The structures explain how the heterophilic Ig1-Ig4 horseshoe’s in the contactin 1 – neurofascin 155 complex define the 7.4 nm paranodal spacing and how the remaining six domains enable bridging of distinct intercellular distances.

Suggested Citation

  • Lucas M. P. Chataigner & Christos Gogou & Maurits A. Boer & Cátia P. Frias & Dominique M. E. Thies-Weesie & Joke C. M. Granneman & Albert J. R. Heck & Dimphna H. Meijer & Bert J. C. Janssen, 2022. "Structural insights into the contactin 1 – neurofascin 155 adhesion complex," Nature Communications, Nature, vol. 13(1), pages 1-17, December.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-34302-9
    DOI: 10.1038/s41467-022-34302-9
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    References listed on IDEAS

    as
    1. Matti F. Pronker & Suzanne Lemstra & Joost Snijder & Albert J. R. Heck & Dominique M. E. Thies-Weesie & R. Jeroen Pasterkamp & Bert J. C. Janssen, 2016. "Structural basis of myelin-associated glycoprotein adhesion and signalling," Nature Communications, Nature, vol. 7(1), pages 1-13, December.
    2. Yinghao Wu & Jeremie Vendome & Lawrence Shapiro & Avinoam Ben-Shaul & Barry Honig, 2011. "Transforming binding affinities from three dimensions to two with application to cadherin clustering," Nature, Nature, vol. 475(7357), pages 510-513, July.
    3. Minou Djannatian & Sebastian Timmler & Martina Arends & Manja Luckner & Marie-Theres Weil & Ioannis Alexopoulos & Nicolas Snaidero & Bettina Schmid & Thomas Misgeld & Wiebke Möbius & Martina Schiffere, 2019. "Two adhesive systems cooperatively regulate axon ensheathment and myelin growth in the CNS," Nature Communications, Nature, vol. 10(1), pages 1-15, December.
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