{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Khan YA"],"funding":["NIMH NIH HHS","NCI NIH HHS","NIGMS NIH HHS","NIH HHS"],"pagination":["1708-1720"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12440825"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["32(9)"],"pubmed_abstract":["SNARE (soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein receptor) proteins drive membrane fusion at different cell compartments as their core domains zipper into a parallel four-helix bundle. After fusion, these bundles are disassembled by the AAA+ (ATPase associated with diverse cellular activities) protein Sec18/NSF and its adaptor Sec17/α-SNAP to make them available for subsequent rounds of membrane fusion. SNARE domains are often flanked by C-terminal transmembrane or N-terminal domains. Previous structures of the NSF-α-SNAP-SNARE complex revealed binding to the D1 ATPase pore, posing a topological constraint as SNARE transmembrane domains would prevent complete substrate threading as suggested for other AAA+ systems. Using mass spectrometry in yeast cells, we show N-"],"journal":["Nature structural & molecular biology"],"pubmed_title":["SNARE disassembly requires Sec18/NSF side loading."],"pmcid":["PMC12440825"],"funding_grant_id":["S10 OD030473","P30 CA124435","F31 MH134477","R35 GM118037","R01 MH063105"],"pubmed_authors":["Mckenzie G","Singal B","Montabana E","Esquivies L","Khan YA","Mclaughlin T","Choi UB","Pfuetzner RA","DeLong K","Brunger AT","Wickner WT","White KI","Liu F"],"additional_accession":[]},"is_claimable":false,"name":"SNARE disassembly requires Sec18/NSF side loading.","description":"SNARE (soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein receptor) proteins drive membrane fusion at different cell compartments as their core domains zipper into a parallel four-helix bundle. After fusion, these bundles are disassembled by the AAA+ (ATPase associated with diverse cellular activities) protein Sec18/NSF and its adaptor Sec17/α-SNAP to make them available for subsequent rounds of membrane fusion. SNARE domains are often flanked by C-terminal transmembrane or N-terminal domains. Previous structures of the NSF-α-SNAP-SNARE complex revealed binding to the D1 ATPase pore, posing a topological constraint as SNARE transmembrane domains would prevent complete substrate threading as suggested for other AAA+ systems. Using mass spectrometry in yeast cells, we show N-","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Sep","modification":"2026-06-03T08:00:58.524Z","creation":"2026-04-26T03:12:05.632Z"},"accession":"S-EPMC12440825","cross_references":{"pubmed":["40604310"],"doi":["10.1038/s41594-025-01590-w"]}}