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TitleStructurally exclusive Teneurin complexes orchestrate divergent programs in early cortical development.
Journal, issue, pagesNat Commun, Vol. 17, Issue 1, Year 2026
Publish dateApr 16, 2026
AuthorsMiguel Berbeira-Santana / Claudia Peregrina / Kosuke Okuda / Jin Chuan Zhou / Maria Carrasquero-Ordaz / Amy V Roberts / Anne E Thomas / Evert Haanappel / Matthieu Chavent / Kamel El Omari / Lindsay A Baker / Daniel T Pederick / Els Pardon / Jan Steyaert / U Valentin Nägerl / Daniel Del Toro / Elena Seiradake /
PubMed AbstractCortical migration is a complex process in which neurons migrate along radial glial cells (RGC) to form functional layers. Teneurins (Ten1-4) play a role by interacting with Latrophilins (Lphn/ADGRL1- ...Cortical migration is a complex process in which neurons migrate along radial glial cells (RGC) to form functional layers. Teneurins (Ten1-4) play a role by interacting with Latrophilins (Lphn/ADGRL1-3). Teneurins are also known as cell adhesion molecules, but how homophilic and heterophilic Teneurin interactions are integrated is unknown. Here, single-particle-cryo-EM data of Ten2 shows that canonical Latrophilin-binding is sterically incompatible with Ten2-dimerisation, making these interactions exclusive. We engineered surface mutations that specifically disrupt Ten2-Ten2 or Ten2-Latrophilin interactions. These are transferrable to Ten4, suggesting conserved binding mechanisms. Proteomics, in-vivo-gene-editing and super-resolution-microscopy show that Ten4 is expressed along RGC fibres and that migrating neurons switch from low-to-high Ten4-expression. Ten4 expression is highest in the cortical plate where Ten4-Ten4 interactions reduce RGC-attachment. In the intermediate zone, Ten4-Latrophilin interactions are required to promote neuron-RGC association. The results show how Ten4 orchestrates different stages of cortical migration by using a structural/functional switch between high-affinity Lphn interactions and low-affinity homophilic interactions, underpinning the integration of distinct migration programmes.
External linksNat Commun / PubMed:41991904 / PubMed Central
MethodsEM (single particle)
Resolution2.55 - 3.48 Å
Structure data

50975

9g2f

EMDB-50975, PDB-9g2f:
Mouse Teneurin2 dimer variant A1B1
Method: EM (single particle) / Resolution: 2.8 Å

50976

9g2h

EMDB-50976, PDB-9g2h:
Mouse Teneurin2 dimer variant A1B0
Method: EM (single particle) / Resolution: 2.55 Å

51021

9g41

EMDB-51021, PDB-9g41:
Mouse Teneurin2 dimer variant A0B1
Method: EM (single particle) / Resolution: 3.48 Å

51022

9g42

EMDB-51022, PDB-9g42:
Mouse Teneurin2 dimer variant A0B0
Method: EM (single particle) / Resolution: 2.82 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • mus musculus (house mouse)
KeywordsCELL ADHESION / cell adhesion molecule / complex / homodimer

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