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Alternative splicing controls teneurin-3 compact dimer formation for neuronal recognition.

Christos Gogou1, J Wouter Beugelink2, Cátia P Frias1

  • 1Department of Bionanoscience, Kavli Institute of Nanoscience Delft, Delft University of Technology, van der Maasweg 9, Delft, the Netherlands.

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Alternative splicing of teneurin-3 cell adhesion molecules creates distinct dimeric structures. These structures mediate specific neuronal recognition, influencing the wiring of neuronal circuits.

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Structural Biology

Background:

  • Neuronal network formation relies on cell adhesion molecules.
  • Alternative splicing of these molecules adds specificity to neuronal connections.

Purpose of the Study:

  • To elucidate the structural basis of teneurin-3 alternative splicing.
  • To understand how splice variants influence teneurin interactions and neuronal wiring.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) to determine structures of teneurin-3 isoforms.
  • Small-angle X-ray scattering (SAXS) and negative stain EM for structural analysis.
  • Cell clustering and stripe assays to assess trans-cellular interactions.

Main Results:

  • Identified compact dimeric ectodomain structures for teneurin-3 isoforms.
  • Demonstrated that an EGF8-ABD contact stabilizes the dimer.
  • Revealed variant-specific dimeric arrangements influencing trans-cellular interactions.
  • Showcased how alternative splicing alters subunit arrangements in teneurin dimers.

Conclusions:

  • Alternative splicing of teneurin-3 leads to rearrangements in dimeric subunit organization.
  • These structural changes provide a basis for specific teneurin homo- and heterophilic interactions.
  • Findings offer insights into how teneurins contribute to neuronal recognition and circuit wiring.