How Synaptotagmin Promotes Membrane Fusion
Abstract
Synaptic vesicles loaded with neurotransmitters are exocytosed in a soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE)-dependent manner after presynaptic depolarization induces calcium ion (Ca2+) influx. The Ca2+ sensor required for fast fusion is synaptotagmin-1. The activation energy of bilayer-bilayer fusion is very high (approximately 40 k(B)T). We found that, in response to Ca2+ binding, synaptotagmin-1 could promote SNARE-mediated fusion by lowering this activation barrier by inducing high positive curvature in target membranes on C2-domain membrane insertion. Thus, synaptotagmin-1 triggers the fusion of docked vesicles by local Ca2+-dependent buckling of the plasma membrane together with the zippering of SNAREs. This mechanism may be widely used in membrane fusion.
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Upon Ca2+ binding to the Syt1 C2B domain, the Ca2+ binding loops partially insert into the membrane with a preference for membrane curvature, possibly supported by ionic interactions via the polybasic region and with continuing maintenance of the Syt1-SNARE interface.
“Upon Ca2+ binding to the Syt1 C2B domain, the Ca2+ binding loops partially insert into the membrane23 with a preference for membrane curvature20,21, possibly supported by ionic interactions via the polybasic region and with continuing maintenance of the Syt1-SNARE interface.”
From Architecture of the synaptotagmin–SNARE machinery for neuronal exocytosis (2015) · cites this paper as [21]
Increased ensemble lipid mixing was observed upon addition of the soluble Syt1 C2AB fragment and Ca2+.
“For example, increased ensemble lipid mixing was observed upon addition of the soluble Syt1 C2AB fragment and Ca2+ (ref. 21).”
From Architecture of the synaptotagmin–SNARE machinery for neuronal exocytosis (2015) · cites this paper as [21]
Previous reconstitutions often employed lipid mixing, rather than content mixing, between vesicles with reconstituted neuronal SNAREs.
“Previous reconstitutions often employed lipid mixing, rather than content mixing, between vesicles with reconstituted neuronal SNAREs21,83.”
From Architecture of the synaptotagmin–SNARE machinery for neuronal exocytosis (2015) · cites this paper as [21]
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References 26 · Cited by 528
- Authors
- Martens, S., Kozlov, M. M., & McMahon, H. T.
- Affiliations
- Tel Aviv University (IL)
- Corresponding author
- McMahon, Harvey T.
- Venue
- Science
- Published
- 2007-05-25
- Volume
- 316
- Issue
- 5828
- Pages
- 1205-1208
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2072023677
- Cited by
- 528
- References
- 26
- Citations by year
- 2026: 4 · 2025: 7 · 2024: 14 · 2023: 13 · 2022: 31 · 2021: 16 · 2020: 19 · 2019: 19 · 2018: 20 · 2017: 23 · 2016: 18 · 2015: 38 · 2014: 35 · 2013: 23 · 2012: 39
- FWCI
- 21.88
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Keywords
- synaptotagmin-1, membrane fusion, SNARE complex, synaptic vesicle exocytosis, calcium binding, C2 domain, membrane curvature, activation energy, membrane buckling, neurotransmitter release
- MeSH terms
- Animals, Calcium, Cell Membrane, Exocytosis, Humans, Liposomes, Membrane Fusion, Models, Biological, Synaptic Vesicles, SNARE Proteins, Synaptotagmin I, Rats
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