Distinct Initial SNARE Configurations Underlying the Diversity of Exocytosis
Abstract
The dynamics of exocytosis are diverse and have been optimized for the functions of synapses and a wide variety of cell types. For example, the kinetics of exocytosis varies by more than five orders of magnitude between ultrafast exocytosis in synaptic vesicles and slow exocytosis in large dense-core vesicles. However, in all cases, exocytosis is mediated by the same fundamental mechanism, i.e., the assembly of soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins. It is often assumed that vesicles need to be docked at the plasma membrane and SNARE proteins must be preassembled before exocytosis is triggered. However, this model cannot account for the dynamics of exocytosis recently reported in synapses and other cells. For example, vesicles undergo exocytosis without prestimulus docking during tonic exocytosis of synaptic vesicles in the active zone. In addition, epithelial and hematopoietic cells utilize cAMP and kinases to trigger slow exocytosis of nondocked vesicles. In this review, we summarize the manner in which the diversity of exocytosis reflects the initial configurations of SNARE assembly, including trans-SNARE, binary-SNARE, unitary-SNARE, and cis-SNARE configurations. The initial SNARE configurations depend on the particular SNARE subtype (syntaxin, SNAP25, or VAMP), priming proteins (Munc18, Munc13, CAPS, complexin, or snapin), triggering proteins (synaptotagmins, Doc2, and various protein kinases), and the submembraneous cytoma…
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RIM is a binding partner of Rab3 and plays a key role in vesicle docking.
“RIM is a binding partner of the vesicular protein Rab3 (336) and plays a key role in vesicle docking.”
From Pancreatic β-Cell Electrical Activity and Insulin Secretion: Of Mice and Men (2018) · cites this paper as [336]
All the essential proteins required for synaptic vesicle release are also expressed in the β-cell and presumably fulfill the same function(s).
“All the essential proteins required for synaptic vesicle release are also expressed in the β-cell and presumably fulfill the same function(s) (193, 336, 364).”
From Pancreatic β-Cell Electrical Activity and Insulin Secretion: Of Mice and Men (2018) · cites this paper as [336]
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BackgroundSelf-citation
- Authors
- Kasai, H., Takahashi, N., & Tokumaru, H.
- Affiliations
- Center for Disease Biology and Integrative Medicine, The University of Tokyo (JP)
- Corresponding author
- Kasai, Haruo
- Venue
- Physiological Reviews
- Publisher
- American Physiological Society
- Published
- 2012-10
- Volume
- 92
- Issue
- 4
- Pages
- 1915-1964
- ISSN
- 0031-9333 (ISSN-L)
- 1522-1210
- OpenAlex
- W2128495983
- Cited by
- 150
- References
- 19
- Citations by year
- 2026: 1 · 2025: 7 · 2024: 5 · 2023: 7 · 2022: 15 · 2021: 9 · 2020: 4 · 2019: 4 · 2018: 7 · 2017: 20 · 2016: 13 · 2015: 25 · 2014: 17 · 2013: 16
- FWCI
- 1.71
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Physiological Reviews (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Japan Society for the Promotion of Science (21000009)
- Topics
- 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
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Keywords
- exocytosis, SNARE proteins, synaptic vesicles, dense core vesicles, vesicle docking, Munc18, Munc13, CAPS, complexin, synaptotagmin, protein kinases, cAMP signaling, membrane trafficking, exocytosis kinetics, synaptic active zone
- MeSH terms
- Animals, Exocytosis, Protein Conformation, Synapses, Synaptic Vesicles, SNARE Proteins
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