ArticleMolecular biology of the cell2022
Sec18 supports membrane fusion by promoting Sec17 membrane association.
Article in Molecular biology of the cell, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 14 citations in OpenAlex.
- Functional assembly of the Qc-SNARE with Sec18 and Sec17 on membranes.Molecular biology of the cell · 2026Article
- SNARE disassembly requires Sec18/NSF side loading.Nature structural & molecular biology · 2025Article
- Sec18 ATP hydrolysis selectively releases Sec17 fromMolecular biology of the cell · 2025Article
- SNARE disassembly requires Sec18/NSF side-loading.bioRxiv : the preprint server for biology · 2025Article
- After their membrane assembly, Sec18 (NSF) and Sec17 (SNAP) promote membrane fusion.Molecular biology of the cell · 2024Article
- Membrane fusion reactions limited by defective SNARE zippering or stiff lipid fatty acyl composition have distinct requirements for Sec17, Sec18, and adenine nucleotide.bioRxiv : the preprint server for biology · 2024Article
- Sec18 binds the tethering/SM complex HOPS to engage the Qc-SNARE for membrane fusion.Molecular biology of the cell · 2024Article
- MARCKS Effector Domain, a reversible lipid ligand, illuminates late stages of membrane fusion.Molecular biology of the cell · 2023Article
- Efficient fusion requires a membrane anchor on the vacuolar Qa-SNARE.Molecular biology of the cell · 2023Article
- PI3P regulates multiple stages of membrane fusion.Molecular biology of the cell · 2023Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Membrane fusion is driven by Sec17, Sec18, and SNARE zippering. Sec17 bound to SNAREs promotes fusion through its membrane-proximal N-terminal apolar loop domain. At its membrane-distal end, Sec17 serves as a high-affinity receptor for Sec18. At that distance from the fusion site, it has been unclear how Sec18 can aid Sec17 to promote fusion. We now report that Sec18, with ATPγS, lowers the Km of Sec17 for fusion. A C-terminal and membrane-distal Sec17 mutation, L291A,L292A, diminishes Sec17 affinity for Sec18. High levels of wild-type Sec17 or Sec17-L291AL292A show equivalent fusion without Sec18, but Sec18 causes far less fusion enhancement with low levels of Sec17-L291AL292A than with wild-type Sec17. Another mutant, Sec17-F21SM22S, has reduced N-loop apolarity. Only very high levels of this mutant protein support fusion, but Sec18 still lowers the apparent fusion Km for Sec17-F21SM22S. Thus Sec18 stimulates fusion through Sec17 and acts at the well-described interface between Sec18 and Sec17. ATP acts as a ligand to activate Sec18 for Sec17-dependent fusion, but ATP hydrolysis is not required. Even without SNAREs, Sec18 and Sec17 exhibit interdependent stable association with lipids, with several Sec17 bound for each Sec18 hexamer, explaining how Sec18 stabilization of surface-concentrated clusters of Sec17 lowers the Sec17 Km for assembly with SNAREs. Each of the associations, between SNARE complex, Sec18, Sec17, and lipid, helps assemble the fusion machinery.
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