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: Jingxian Li, Yuan Xie, Shaleeka Cornelius, Xian Jiang, Richard Sando, Szymon P. Kordon, Man Pan, Katherine Leon, Thomas C. Südhof, Minglei Zhao, Demet Araç
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2020
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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.