ArticleeLife2014
Common intermediates and kinetics, but different energetics, in the assembly of SNARE proteins.
Article in eLife, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
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Who cites it
54 citing papers in PubMed.
- SM protein Sly1 and a SNARE Habc domain promote membrane fusion through multiple mechanisms.The Journal of cell biology · 2024Article
- Dual-Ring SNAREpin Machinery Tuning for Fast Synaptic Vesicle Fusion.Biomolecules · 2024Article
- Tomosyns attenuate SNARE assembly and synaptic depression by binding to VAMP2-containing template complexes.Nature communications · 2024Article
- SNARE Proteins in Synaptic Vesicle Fusion.Advances in neurobiology · 2023Article
- A dynamic template complex mediates Munc18-chaperoned SNARE assembly.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Neuronal SNARE complex assembly guided by Munc18-1 and Munc13-1.FEBS open bio · 2022Review
- The beginning and the end of SNARE-induced membrane fusion.FEBS open bio · 2022Review
- Stability profile of the neuronal SNARE complex reflects its potency to drive fast membrane fusion.Biophysical journal · 2022Article
- Energetics, kinetics, and pathways of SNARE assembly in membrane fusion.Critical reviews in biochemistry and molecular biology · 2022Review
- Article
- Stepwise membrane binding of extended synaptotagmins revealed by optical tweezers.Nature chemical biology · 2022Article
- Nano-Precision Tweezers for Mechanosensitive Proteins and Beyond.Molecules and cells · 2022Review
- Quantitative Models of Lipid Transfer and Membrane Contact Formation.Contact (Thousand Oaks (Ventura County, Calif.)) · 2022Article
- Chaperoning SNARE Folding and Assembly.Annual review of biochemistry · 2021Review
- Article
- SNARE Regulatory Proteins in Synaptic Vesicle Fusion and Recycling.Frontiers in molecular neuroscience · 2021Review
- Arrangements of proteins at reconstituted synaptic vesicle fusion sites depend on membrane separation.FEBS letters · 2020Article
- Resolving kinetic intermediates during the regulated assembly and disassembly of fusion pores.Nature communications · 2020Article
- Energetic dependencies dictate folding mechanism in a complex protein.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- The inner workings of intracellular heterotypic and homotypic membrane fusion mechanisms.Journal of biosciences · 2019Article
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
Soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) are evolutionarily conserved machines that couple their folding/assembly to membrane fusion. However, it is unclear how these processes are regulated and function. To determine these mechanisms, we characterized the folding energy and kinetics of four representative SNARE complexes at a single-molecule level using high-resolution optical tweezers. We found that all SNARE complexes assemble by the same step-wise zippering mechanism: slow N-terminal domain (NTD) association, a pause in a force-dependent half-zippered intermediate, and fast C-terminal domain (CTD) zippering. The energy release from CTD zippering differs for yeast (13 kBT) and neuronal SNARE complexes (27 kBT), and is concentrated at the C-terminal part of CTD zippering. Thus, SNARE complexes share a conserved zippering pathway and polarized energy release to efficiently drive membrane fusion, but generate different amounts of zippering energy to regulate fusion kinetics.
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Registered trials
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