{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Wang C"],"funding":["NIMH NIH HHS","NCI NIH HHS","NIGMS NIH HHS"],"pagination":["899-904"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11269182"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["631(8022)"],"pubmed_abstract":["Synaptic vesicles are organelles with a precisely defined protein and lipid composition<sup>1,2</sup>, yet the molecular mechanisms for the biogenesis of synaptic vesicles are mainly unknown. Here we discovered a well-defined interface between the synaptic vesicle V-ATPase and synaptophysin by in situ cryo-electron tomography and single-particle cryo-electron microscopy of functional synaptic vesicles isolated from mouse brains<sup>3</sup>. The synaptic vesicle V-ATPase is an ATP-dependent proton pump that establishes the proton gradient across the synaptic vesicle, which in turn drives the uptake of neurotransmitters<sup>4,5</sup>. Synaptophysin<sup>6</sup> and its paralogues synaptoporin<sup>7</sup> and synaptogyrin<sup>8</sup> belong to a family of abundant synaptic vesicle proteins who"],"journal":["Nature"],"pubmed_title":["Structure and topography of the synaptic V-ATPase-synaptophysin complex."],"pmcid":["PMC11269182"],"funding_grant_id":["R01 GM114496","P30 CA124435","T32 GM065103","R01 MH063105"],"pubmed_authors":["Jiang L","Stowell MHB","Yang K","Esquivies L","Jian R","Wang C","Guo Q","Hampton L","Brunger AT","Leitz J","Adams DJ","Jiang W","Basta T","Held RG","Wang X","Baumeister W","Shen X"],"additional_accession":[]},"is_claimable":false,"name":"Structure and topography of the synaptic V-ATPase-synaptophysin complex.","description":"Synaptic vesicles are organelles with a precisely defined protein and lipid composition<sup>1,2</sup>, yet the molecular mechanisms for the biogenesis of synaptic vesicles are mainly unknown. Here we discovered a well-defined interface between the synaptic vesicle V-ATPase and synaptophysin by in situ cryo-electron tomography and single-particle cryo-electron microscopy of functional synaptic vesicles isolated from mouse brains<sup>3</sup>. The synaptic vesicle V-ATPase is an ATP-dependent proton pump that establishes the proton gradient across the synaptic vesicle, which in turn drives the uptake of neurotransmitters<sup>4,5</sup>. Synaptophysin<sup>6</sup> and its paralogues synaptoporin<sup>7</sup> and synaptogyrin<sup>8</sup> belong to a family of abundant synaptic vesicle proteins who","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Jul","modification":"2026-04-29T23:57:47.879Z","creation":"2025-04-19T13:09:52.363Z"},"accession":"S-EPMC11269182","cross_references":{"pubmed":["38838737"],"doi":["10.1038/s41586-024-07610-x"]}}