ArticleProceedings of the National Academy of Sciences of the United States of America2016
Kinetic barriers to SNAREpin assembly in the regulation of membrane docking/priming and fusion.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 56 citations in OpenAlex.
- Synaptic transmission: Munc13 assembles onto PI(4,5)PProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Independently engaging protein tethers of different length enhance synaptic vesicle trafficking to the plasma membrane.The Journal of physiology · 2025Article
- Quantitative single-molecule analysis of assembly and CaCommunications biology · 2024Article
- Intermediate steps in the formation of neuronal SNARE complexes.The Journal of biological chemistry · 2024Article
- Diacylglycerol-dependent hexamers of the SNARE-assembling chaperone Munc13-1 cooperatively bind vesicles.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- The Role of Tomosyn in the Regulation of Neurotransmitter Release.Advances in neurobiology · 2023Article
- SNARE Proteins in Synaptic Vesicle Fusion.Advances in neurobiology · 2023Article
- The beginning and the end of SNARE-induced membrane fusion.FEBS open bio · 2022Review
- Synaptotagmin rings as high-sensitivity regulators of synaptic vesicle docking and fusion.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Stability profile of the neuronal SNARE complex reflects its potency to drive fast membrane fusion.Biophysical journal · 2022Article
- Article
- Energetics, kinetics, and pathways of SNARE assembly in membrane fusion.Critical reviews in biochemistry and molecular biology · 2022Review
- Synaptic Secretion and Beyond: Targeting Synapse and Neurotransmitters to Treat Neurodegenerative Diseases.Oxidative medicine and cellular longevity · 2022Review
- Munc18-dependent and -independent clustering of syntaxin in the plasma membrane of cultured endocrine cells.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Chaperoning SNARE Folding and Assembly.Annual review of biochemistry · 2021Review
- AtSEC22 Regulates Cell Morphogenesis via Affecting Cytoskeleton Organization and Stabilities.Frontiers in plant science · 2021Article
- Synergistic roles of Synaptotagmin-1 and complexin in calcium-regulated neuronal exocytosis.eLife · 2020Article
- SRRF-Stream Imaging of Optogenetically Controlled Furrow Formation Shows Localized and Coordinated Endocytosis and Exocytosis Mediating Membrane Remodeling.ACS synthetic biology · 2020Article
- Structural dynamics and transient lipid binding of synaptobrevin-2 tune SNARE assembly and membrane fusion.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Diverse Role of SNARE Protein Sec22 in Vesicle Trafficking, Membrane Fusion, and Autophagy.Cells · 2019Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Neurotransmission is achieved by soluble NSF attachment protein receptor (SNARE)-driven fusion of readily releasable vesicles that are docked and primed at the presynaptic plasma membrane. After neurotransmission, the readily releasable pool of vesicles must be refilled in less than 100 ms for subsequent release. Here we show that the initial association of SNARE complexes, SNAREpins, is far too slow to support this rapid refilling owing to an inherently high activation energy barrier. Our data suggest that acceleration of this process, i.e., lowering of the barrier, is physiologically necessary and can be achieved by molecular factors. Furthermore, under zero force, a low second energy barrier transiently traps SNAREpins in a half-zippered state similar to the partial assembly that engages calcium-sensitive regulatory machinery. This result suggests that the barrier must be actively raised in vivo to generate a sufficient pause in the zippering process for the regulators to set in place. We show that the heights of the activation energy barriers can be selectively changed by molecular factors. Thus, it is possible to modify, both in vitro and in vivo, the lifespan of each metastable state. This controllability provides a simple model in which vesicle docking/priming, an intrinsically slow process, can be substantially accelerated. It also explains how the machinery that regulates vesicle fusion can be set in place while SNAREpins are trapped in a half-zippered state.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.