The DOI matches its Crossref record; 104 of the 104 references it cites were found in a registry or an index.
The Morphological and Molecular Nature of Synaptic Vesicle Priming at Presynaptic Active Zones
Open accessAbstract
Synaptic vesicle docking, priming, and fusion at active zones are orchestrated by a complex molecular machinery. We employed hippocampal organotypic slice cultures from mice lacking key presynaptic proteins, cryofixation, and three-dimensional electron tomography to study the mechanism of synaptic vesicle docking in the same experimental setting, with high precision, and in a near-native state. We dissected previously indistinguishable, sequential steps in synaptic vesicle active zone recruitment (tethering) and membrane attachment (docking) and found that vesicle docking requires Munc13/CAPS family priming proteins and all three neuronal SNAREs, but not Synaptotagmin-1 or Complexins. Our data indicate that membrane-attached vesicles comprise the readily releasable pool of fusion-competent vesicles and that synaptic vesicle docking, priming, and trans-SNARE complex assembly are the respective morphological, functional, and molecular manifestations of the same process, which operates downstream of vesicle tethering by active zone components.
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“For example, the readily releasable pool (RRP) often closely correlates with the pool of docked vesicles (i.e., vesicles in the direct contact with AZ plasma membrane) [14] but exceptions to this correlation have been also observed [15–17].”
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 [14]
In the citing paper
“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 [14]
In the citing paper
“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 [14]
Citations
Cites
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SNAREs — engines for membrane fusion
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Synaptotagmin I: A major Ca2+ sensor for transmitter release at a central synapse
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Self-citationNeurotransmitter Release: The Last Millisecond in the Life of a Synaptic Vesicle
Südhof, T. C. (2013) · Neuron · doi:10.1016/j.neuron.2013.10.022 · Cited by 1,197
Self-citationDefinition of the readily releasable pool of vesicles at hippocampal synapses.
Rosenmund, C., & Stevens, C. (1996) · Neuron · doi:10.1016/s0896-6273(00)80146-4 · Cited by 1,084
Self-citationMolecular machines governing exocytosis of synaptic vesicles
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Quantitative ultrastructural analysis of hippocampal excitatory synapses
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Biederer, T., Kaeser, P. S., & Blanpied, T. A. (2017) · Neuron · doi:10.1016/j.neuron.2017.10.006 · Cited by 352
The 2018 biomembrane curvature and remodeling roadmap
Bassereau, P. M., Jin, R., Baumgart, T., Deserno, M., Dimova, R., Frolov, V. A., Bashkirov, P. V., Grubmüller, H., Jahn, R., Risselada, H. J., et al. (2018) · Journal of Physics D Applied Physics · doi:10.1088/1361-6463/aacb98 · Cited by 249
Mechanisms of SNARE proteins in membrane fusion
Jahn, R., Cafiso, D. C., & Tamm, L. K. (2024) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-023-00668-x · Cited by 248
Molecular Mechanisms of Synaptic Vesicle Priming by Munc13 and Munc18
Lai, Y., Choi, U. B., Leitz, J., Rhee, H. J., Lee, C., Altas, B., Zhao, M., Pfuetzner, R. A., Wang, A. L., Brose, N., et al. (2017) · Neuron · doi:10.1016/j.neuron.2017.07.004 · Cited by 235
Self-citationSynaptic weight set by Munc13-1 supramolecular assemblies
Sakamoto, H., Ariyoshi, T., Kimpara, N., Sugao, K., Taiko, I., Takikawa, K., Asanuma, D., Namiki, S., & Hirose, K. (2018) · Nature Neuroscience · doi:10.1038/s41593-017-0041-9 · Cited by 235
Metadata
- Authors
- Imig, C., Min, S.-W., Krinner, S., Arancillo, M., Rosenmund, C., Südhof, T. C., Rhee, J., Brose, N., & Cooper, B. H.
- Affiliations
- Max Planck Institute of Experimental Medicine (DE)
- NeuroCure Cluster of Excellence (DE)
- Howard Hughes Medical Institute (US)
- Corresponding author
- Brose, Nils
- Cooper, Benjamin H.
- ORCID
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 2014-10
- Volume
- 84
- Issue
- 2
- Pages
- 416-431
- ISSN
- 0896-6273 (ISSN-L)
- OpenAlex
- W1996414800
- Cited by
- 389
- References
- 104
- Citations by year
- 2026: 18 · 2025: 24 · 2024: 33 · 2023: 28 · 2022: 42 · 2021: 44 · 2020: 35 · 2019: 39 · 2018: 32 · 2017: 40 · 2016: 27 · 2015: 26 · 2014: 1
- FWCI
- 15.60
- Type
- journal article
- Language
- en
- Update notices
- erratum (2014-11-19)
- Open access
- bronze
- doi.org
- Licence
- Locations
- Neuron (publishedVersion)
- PubMed (publishedVersion)
- Max Planck Institute for Plasma Physics (submittedVersion)
- GRO (submittedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion)
- Funders
- Howard Hughes Medical Institute
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Extracellular vesicles in disease
- Keywords
- synaptic vesicle priming, synaptic vesicle docking, active zone, Munc13, synaptotagmin-1, complexin, vesicle tethering, membrane adhesion, readily releasable pool, hippocampal synapses
- MeSH terms
- Animals, Hippocampus, Membrane Fusion, Synaptic Transmission, Neurons, Synapses, Synaptic Vesicles, SNARE Proteins, Mice
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