LRRTM2 controls presynapse nano-organization and AMPA receptor sub-positioning through Neurexin-binding interface

Konstantina Liouta, Malgorzata Lubas, Vasika Venugopal, Julia Chabbert, Caroline Jeannière, Candice Diaz, Matthieu Munier, Béatrice Tessier, Stéphane Claverol, Alexandre Favereaux, Matthieu Sainlos, Joris Wit, Mathieu Letellier, Olivier Thoumine and Ingrid Chamma ()
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Konstantina Liouta: Centre National de la Recherche Scientifique
Malgorzata Lubas: Centre National de la Recherche Scientifique
Vasika Venugopal: Centre National de la Recherche Scientifique
Julia Chabbert: Centre National de la Recherche Scientifique
Caroline Jeannière: Centre National de la Recherche Scientifique
Candice Diaz: Centre National de la Recherche Scientifique
Matthieu Munier: Centre National de la Recherche Scientifique
Béatrice Tessier: Centre National de la Recherche Scientifique
Stéphane Claverol: Bordeaux Proteome
Alexandre Favereaux: Centre National de la Recherche Scientifique
Matthieu Sainlos: Centre National de la Recherche Scientifique
Joris Wit: VIB Center for Brain & Disease Research
Mathieu Letellier: Centre National de la Recherche Scientifique
Olivier Thoumine: Centre National de la Recherche Scientifique
Ingrid Chamma: Centre National de la Recherche Scientifique

Nature Communications, 2024, vol. 15, issue 1, 1-18

Abstract: Abstract Synapses are organized into nanocolumns that control synaptic transmission efficacy through precise alignment of postsynaptic neurotransmitter receptors and presynaptic release sites. Recent evidence show that Leucine-Rich Repeat Transmembrane protein LRRTM2, highly enriched and confined at synapses, interacts with Neurexins through its C-terminal cap, but the role of this binding interface has not been explored in synapse formation and function. Here, we develop a conditional knock-out mouse model (cKO) to address the molecular mechanisms of LRRTM2 regulation, and its role in synapse organization and function. We show that LRRTM2 cKO specifically impairs excitatory synapse formation and function in mice. Surface expression, synaptic clustering, and membrane dynamics of LRRTM2 are tightly controlled by selective motifs in the C-terminal domain. Conversely, the N-terminal domain controls presynapse nano-organization and postsynapse AMPAR sub-positioning and stabilization through the recently identified Neurexin-binding interface. Thus, we identify LRRTM2 as a central organizer of pre- and post- excitatory synapse nanostructure through interaction with presynaptic Neurexins.

Date: 2024
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DOI: 10.1038/s41467-024-53090-y

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