Alternative splicing controls teneurin-latrophilin interaction and synapse specificity by a shape-shifting mechanism
The trans-synaptic interaction of the cell-adhesion molecules teneurins (TENs) with latrophilins (LPHNs) promotes excitatory synapse formation. Here authors report the high resolution cryo-EM structure of the TEN2-LPHN3 complex, describe the trimeric TEN2-LPHN3-FLRT3 complex and show how alternative...
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| Autores principales: | , , , , , , , , , , |
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| Formato: | article |
| Lenguaje: | EN |
| Publicado: |
Nature Portfolio
2020
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| Materias: | |
| Acceso en línea: | https://doaj.org/article/40b62dc45fba43818c436bb498569426 |
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| Sumario: | The trans-synaptic interaction of the cell-adhesion molecules teneurins (TENs) with latrophilins (LPHNs) promotes excitatory synapse formation. Here authors report the high resolution cryo-EM structure of the TEN2-LPHN3 complex, describe the trimeric TEN2-LPHN3-FLRT3 complex and show how alternative-splicing regulates the TEN2-LPHN3 interaction. |
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