{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"submitter":["Held RG"],"funding":["NIMH NIH HHS","NIGMS NIH HHS","NIH HHS"],"pubmed_abstract":["Most synapses in the brain transmit information by the presynaptic release of vesicular glutamate, driving postsynaptic depolarization through AMPA-type glutamate receptors (AMPARs). The nanometer-scale topography of synaptic AMPARs regulates response amplitude by controlling the number of receptors activated by synaptic vesicle fusion. The mechanisms controlling AMPAR topography and their interactions with postsynaptic scaffolding proteins are unclear, as is the spatial relationship between AMPARs and synaptic vesicles. Here, we used cryo-electron tomography to map the molecular topography of AMPARs and visualize their <i>in-situ</i> structure. Clustered AMPARs form structured complexes with postsynaptic scaffolding proteins resolved by sub-tomogram averaging. Sub-synaptic topography mapp"],"journal":["bioRxiv : the preprint server for biology"],"pagination":["2024.10.19.619226"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11507944"],"repository":["biostudies-literature"],"pubmed_title":["<i>In-Situ</i> Structure and Topography of AMPA Receptor Scaffolding Complexes Visualized by CryoET."],"pmcid":["PMC11507944"],"funding_grant_id":["U24 GM139166","R01 MH063105","S10 OD010580"],"pubmed_authors":["Esquivies L","Wang C","Liang J","Held RG","Khan YA","Azubel M","Brunger AT"],"additional_accession":[]},"is_claimable":false,"name":"<i>In-Situ</i> Structure and Topography of AMPA Receptor Scaffolding Complexes Visualized by CryoET.","description":"Most synapses in the brain transmit information by the presynaptic release of vesicular glutamate, driving postsynaptic depolarization through AMPA-type glutamate receptors (AMPARs). The nanometer-scale topography of synaptic AMPARs regulates response amplitude by controlling the number of receptors activated by synaptic vesicle fusion. The mechanisms controlling AMPAR topography and their interactions with postsynaptic scaffolding proteins are unclear, as is the spatial relationship between AMPARs and synaptic vesicles. Here, we used cryo-electron tomography to map the molecular topography of AMPARs and visualize their <i>in-situ</i> structure. Clustered AMPARs form structured complexes with postsynaptic scaffolding proteins resolved by sub-tomogram averaging. Sub-synaptic topography mapp","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Oct","modification":"2026-04-24T03:24:02.669Z","creation":"2025-04-04T02:58:48.685Z"},"accession":"S-EPMC11507944","cross_references":{"pubmed":["39464045"],"doi":["10.1101/2024.10.19.619226"]}}