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• W1992603916 abstract "Recently, leucine-rich repeat transmembrane proteins (LRRTMs) were found to be synaptic cell-adhesion molecules that, when expressed in nonneuronal cells, induce presynaptic differentiation in contacting axons. We now demonstrate that LRRTM2 induces only excitatory synapses, and that it also acts to induce synapses in transfected neurons similarly to neuroligin-1. Using affinity chromatography, we identified α- and β-neurexins as LRRTM2 ligands, again rendering LRRTM2 similar to neuroligin-1. However, whereas neuroligins bind neurexins containing or lacking an insert in splice site #4, LRRTM2 only binds neurexins lacking an insert in splice site #4. Binding of neurexins to LRRTM2 can produce cell-adhesion junctions, consistent with a trans-interaction regulated by neurexin alternative splicing, and recombinant neurexin-1β blocks LRRTM2’s ability to promote presynaptic differentiation. Thus, our data suggest that two unrelated postsynaptic cell-adhesion molecules, LRRTMs and neuroligins, unexpectedly bind to neurexins as the same presynaptic receptor, but that their binding is subject to distinct regulatory mechanisms." @default.
• W1992603916 created "2016-06-24" @default.
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• W1992603916 creator A5063359584 @default.
• W1992603916 creator A5079564536 @default.
• W1992603916 date "2009-12-01" @default.
• W1992603916 modified "2023-10-18" @default.
• W1992603916 title "LRRTM2 Functions as a Neurexin Ligand in Promoting Excitatory Synapse Formation" @default.
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• W1992603916 doi "https://doi.org/10.1016/j.neuron.2009.12.012" @default.
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