{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Zhang X"],"funding":["NIMH NIH HHS"],"pagination":["322-329"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11808628"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["387(6731)"],"pubmed_abstract":["Synapses are organized by trans-synaptic adhesion molecules that coordinate assembly of pre- and postsynaptic specializations, which, in turn, are composed of scaffolding proteins forming liquid-liquid phase-separated condensates. Presynaptic teneurins mediate excitatory synapse organization by binding to postsynaptic latrophilins; however, the mechanism of action of teneurins, driven by extracellular domains evolutionarily derived from bacterial toxins, remains unclear. In this work, we show that only the intracellular sequence, a dimerization sequence, and extracellular bacterial toxin-derived latrophilin-binding domains of Teneurin-3 are required for synapse organization, suggesting that teneurin-induced latrophilin clustering mediates synaptogenesis. Intracellular Teneurin-3 sequences "],"journal":["Science (New York, N.Y.)"],"pubmed_title":["Reconstitution of synaptic junctions orchestrated by teneurin-latrophilin complexes."],"pmcid":["PMC11808628"],"funding_grant_id":["R01 MH126929"],"pubmed_authors":["Zhang X","Sudhof TC","Chen X","Matus D"],"additional_accession":[]},"is_claimable":false,"name":"Reconstitution of synaptic junctions orchestrated by teneurin-latrophilin complexes.","description":"Synapses are organized by trans-synaptic adhesion molecules that coordinate assembly of pre- and postsynaptic specializations, which, in turn, are composed of scaffolding proteins forming liquid-liquid phase-separated condensates. Presynaptic teneurins mediate excitatory synapse organization by binding to postsynaptic latrophilins; however, the mechanism of action of teneurins, driven by extracellular domains evolutionarily derived from bacterial toxins, remains unclear. In this work, we show that only the intracellular sequence, a dimerization sequence, and extracellular bacterial toxin-derived latrophilin-binding domains of Teneurin-3 are required for synapse organization, suggesting that teneurin-induced latrophilin clustering mediates synaptogenesis. Intracellular Teneurin-3 sequences ","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Jan","modification":"2025-04-04T11:57:01.795Z","creation":"2025-04-04T11:57:01.795Z"},"accession":"S-EPMC11808628","cross_references":{"pubmed":["39818903"],"doi":["10.1126/science.adq3586"]}}