| Fusion of tethered membranes can be driven by Sec18/NSF and Sec17/alphaSNAP without HOPS. | Fusion of tethered membranes can be driven by Sec18/NSF and Sec17/αSNAP without HOPS.
Song H, Wickner WT., Free PMC Article | 11/22/2021 |
| We also show that IPA more potently and specifically inhibits NSF/Sec18 activity than does N-ethylmaleimide, requiring the administration of only low micromolar concentrations of IPA, demonstrating that this compound could help to further elucidate SNARE-priming dynamics | A small-molecule competitive inhibitor of phosphatidic acid binding by the AAA+ protein NSF/Sec18 blocks the SNARE-priming stage of vacuole fusion.
Sparks RP, Arango AS, Starr ML, Aboff ZL, Hurst LR, Rivera-Kohr DA, Zhang C, Harnden KA, Jenkins JL, Guida WC, Tajkhorshid E, Fratti RA., Free PMC Article | 06/13/2020 |
| IPA did not interfere with PA binding to another known target or with Sec18 binding to other kinds of lipids or with other steps in the in vitro fusion assay, indicating clear specificity. | New gadget in the membrane trafficking toolbox: A novel inhibitor of SNARE priming.
Abeliovich H., Free PMC Article | 06/13/2020 |
| SNARE-only fusion is abolished by Sec17 and Sec18. Efficient fusion with Sec17 and Sec18 requires a tripartite match between the organellar identities of the R-SNARE, the Q-SNAREs, and the SM protein/complex. Sec17 and Sec18 are not simply negative regulators; they stimulate fusion with either vacuolar SNAREs and their SM protein complex HOPS or endoplasmic reticulum/cis-Golgi SNAREs and their SM protein Sly1. | Sec17 (α-SNAP) and Sec18 (NSF) restrict membrane fusion to R-SNAREs, Q-SNAREs, and SM proteins from identical compartments.
Jun Y, Wickner W., Free PMC Article | 04/25/2020 |
| When SNAREs are more disassembled, as by Sec17, Sec18, and ATP (adenosine triphosphate), HOPS is required, and GST-PX does not suffice. | Tethering guides fusion-competent trans-SNARE assembly.
Song H, Wickner W., Free PMC Article | 03/28/2020 |
| PA regulates Sec18 function by altering its architecture and stabilizing membrane-bound Sec18 protomers | Phosphatidic acid induces conformational changes in Sec18 protomers that prevent SNARE priming.
Starr ML, Sparks RP, Arango AS, Hurst LR, Zhao Z, Lihan M, Jenkins JL, Tajkhorshid E, Fratti RA., Free PMC Article | 05/11/2019 |
| Sec17 and Sec18 act twice in the fusion cycle, binding to trans-SNARE complexes to accelerate fusion, then hydrolyzing ATP to disassemble cis-SNARE complexes. | Sec17/Sec18 act twice, enhancing membrane fusion and then disassembling cis-SNARE complexes.
Song H, Orr A, Duan M, Merz AJ, Wickner W., Free PMC Article | 05/19/2018 |
| In vitro, Sly1 and Vps33 impede SNARE complex disassembly by Sec18 and ATP | SM proteins Sly1 and Vps33 co-assemble with Sec17 and SNARE complexes to oppose SNARE disassembly by Sec18.
Lobingier BT, Nickerson DP, Lo SY, Merz AJ., Free PMC Article | 11/21/2015 |
| Sec17 binds to trans-SNARE complexes, oligomerizes, and inserts apolar loops into the apposed membranes, locally disturbing the lipid bilayer and lowering the energy barrier for fusion without Sec18 | Sec17 can trigger fusion of trans-SNARE paired membranes without Sec18.
Zick M, Orr A, Schwartz ML, Merz AJ, Wickner WT., Free PMC Article | 08/8/2015 |
| Using a reconstituted proteoliposome fusion system, the authors show that trans-SNARE complex, like cis-SNARE complex, is sensitive to Sec17p/Sec18p mediated disassembly. | HOPS prevents the disassembly of trans-SNARE complexes by Sec17p/Sec18p during membrane fusion.
Xu H, Jun Y, Thompson J, Yates J, Wickner W., Free PMC Article | 07/5/2010 |
| Data show that the ternary synergy of phosphoinositides and 2 SNARE chaperone systems (SNARE Vam7p and Sec17p/Sec18p/ATP | Phosphoinositides and SNARE chaperones synergistically assemble and remodel SNARE complexes for membrane fusion.
Mima J, Wickner W., Free PMC Article | 01/21/2010 |
| Data suggest that Sec18p and Vam7p remodel trans-SNARE complexes to permit a lipid-anchored R-SNARE to support yeast vacuole fusion. | Sec18p and Vam7p remodel trans-SNARE complexes to permit a lipid-anchored R-SNARE to support yeast vacuole fusion.
Jun Y, Xu H, Thorngren N, Wickner W., Free PMC Article | 01/21/2010 |
| The ArfGAP Gcs1p accelerates vesicle (v)-target membrane (t)-SNARE complex formation in vitro, indicating that ArfGAPs may act as folding chaperones. | Interaction of SNAREs with ArfGAPs precedes recruitment of Sec18p/NSF.
Schindler C, Spang A., Free PMC Article | 01/21/2010 |