The DOI matches its Crossref record; 61 of the 61 references it cites were found in a registry or an index.
Synaptic weight set by Munc13-1 supramolecular assemblies
Abstract
The weight of synaptic connections, which is controlled not only postsynaptically but also presynaptically, is a key determinant in neuronal network dynamics. The mechanisms controlling synaptic weight, especially on the presynaptic side, remain elusive. Using single-synapse imaging of the neurotransmitter glutamate combined with super-resolution imaging of presynaptic proteins, we identify a presynaptic mechanism for setting weight in central glutamatergic synapses. In the presynaptic terminal, Munc13-1 molecules form multiple and discrete supramolecular self-assemblies that serve as independent vesicular release sites by recruiting syntaxin-1, a soluble N-ethylmaleimide-sensitive-factor attachment receptor (SNARE) protein essential for synaptic vesicle exocytosis. The multiplicity of these Munc13-1 assemblies affords multiple stable states conferring presynaptic weight, potentially encoding several bits of information at individual synapses. Supramolecular assembling enables a stable synaptic weight, which confers robustness of synaptic computation on neuronal circuits and may be a general mechanism by which biological processes operate despite the presence of molecular noise.
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“Furthermore, we discovered that forskolin slightly reduced the distance between CaV2.1 (P/Q-type) Ca2+ channels and Munc13-1, an essential vesicle priming protein and putative marker of primed vesicles [14,40–45].”
From Presynaptic cAMP-PKA-mediated potentiation induces reconfiguration of synaptic vesicle pools and channel-vesicle coupling at hippocampal mossy fiber boutons (2024) · cites this paper as [45]
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“and Munc13-1/2, putative markers of primed vesicles [14,42–45,60,61].”
From Presynaptic cAMP-PKA-mediated potentiation induces reconfiguration of synaptic vesicle pools and channel-vesicle coupling at hippocampal mossy fiber boutons (2024) · cites this paper as [45]
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Molecular Mechanisms Underlying Neurotransmitter Release
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Sensory Processing at Ribbon Synapses in the Retina and the Cochlea
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Metadata
- Authors
- Sakamoto, H., Ariyoshi, T., Kimpara, N., Sugao, K., Taiko, I., Takikawa, K., Asanuma, D., Namiki, S., & Hirose, K.
- Affiliations
- The University of Tokyo (JP)
- Corresponding author
- Hirose, Kenzo
- Venue
- Nature Neuroscience
- Published
- 2017-12-11
- Volume
- 21
- Issue
- 1
- Pages
- 41-49
- ISSN
- 1097-6256 (ISSN-L)
- 1546-1726
- OpenAlex
- W2772190072
- Cited by
- 235
- References
- 61
- Citations by year
- 2026: 21 · 2025: 27 · 2024: 33 · 2023: 26 · 2022: 34 · 2021: 32 · 2020: 31 · 2019: 18 · 2018: 11 · 2017: 2
- FWCI
- 8.30
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Nature Neuroscience (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Japan Society for the Promotion of Science (17K08584, 17H04029)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Extracellular vesicles in disease
- Keywords
- synaptic weights, Munc13-1, supramolecular self-assembly, presynaptic terminals, glutamate release, syntaxin-1, SNARE proteins, synaptic vesicle exocytosis, glutamatergic synapses, super-resolution imaging
- MeSH terms
- Animals, Calcium, Cells, Cultured, Cytoskeletal Proteins, Embryo, Mammalian, Exocytosis, Hippocampus, Nerve Tissue Proteins, Synaptic Transmission, Neurons, Neuropeptides, Synapses, Synaptic Vesicles, Rats, Sprague-Dawley, Presynaptic Terminals, Glutamic Acid, GTP-Binding Proteins, RNA, Small Interfering, Adaptor Proteins, Signal Transducing, Vesicular Glutamate Transport Protein 1, Syntaxin 1, Rats
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