Structural insights into the contactin 1 – neurofascin 155 adhesion complex

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 and Bert J. C. Janssen ()
Additional contact information
Lucas M. P. Chataigner: Utrecht University
Christos Gogou: Delft University of Technology
Maurits A. Boer: Utrecht University
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
Dimphna H. Meijer: Delft University of Technology
Bert J. C. Janssen: Utrecht University

Nature Communications, 2022, vol. 13, issue 1, 1-17

Abstract: 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.

Date: 2022
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DOI: 10.1038/s41467-022-34302-9

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