The DOI matches its Crossref record; 41 of the 41 references it cites were found in a registry or an index.
Differential Control of the Releasable Vesicle Pools by SNAP-25 Splice Variants and SNAP-23
Open accessAbstract
The SNARE complex, consisting of synaptobrevin, syntaxin, and SNAP-25, is essential for calcium-triggered exocytosis in neurosecretory cells. Little is known, however, about how developmentally regulated isoforms and other cognate SNARE components regulate vesicular fusion. To address this question, we examined neuroexocytosis from chromaffin cells of Snap25 null mice rescued by the two splice variants SNAP-25a and SNAP-25b and the ubiquitously expressed homolog SNAP-23. In the absence of SNAP-25, vesicle docking persisted, but primed vesicle pools were empty and fast calcium-triggered release abolished. Single vesicular fusion events showed normal characteristics, except for a shorter duration of the fusion pore. Overexpression of SNAP-25a, SNAP-25b, and SNAP-23 resulted in three distinct phenotypes; SNAP-25b induced larger primed vesicle pools than SNAP-25a, whereas SNAP-23 did not support a standing pool of primed vesicles. We conclude that three alternative SNARE components support exocytosis, but they differ in their ability to stabilize vesicles in the primed state.
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“that show differences in the kinetics of synaptic vesicle release138,139.”
From The neurogenetics of alternative splicing (2016) · cites this paper as [138]
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“the gene for the SNARE protein SNAP25 uses a pair of mutually exclusive exons (5a and 5b) to produce two alternative isoforms”
From The neurogenetics of alternative splicing (2016) · cites this paper as [138]
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Cites
SNAP receptors implicated in vesicle targeting and fusion
Söllner, T. H., Whiteheart, S. W., Brunner, M., Erdjument‐Bromage, H., Geromanos, S. J., Tempst, P., & Rothman, J. E. (1993) · Nature · doi:10.1038/362318a0 · Cited by 3,239
Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution
Sutton, R. B., Fasshauer, D., Jahn, R., & Brunger, A. T. (1998) · Nature · doi:10.1038/26412 · Cited by 2,417
Synaptotagmin I: A major Ca2+ sensor for transmitter release at a central synapse
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Co‐operative action of calcium ions in transmitter release at the neuromuscular junction
Dodge, F. A., & Rahamimoff, R. (1967) · The Journal of Physiology · doi:10.1113/jphysiol.1967.sp008367 · Cited by 1,315
Membrane fusion and exocytosis.
Jahn, R., & Südhof, T. (1999) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.68.1.863 · Cited by 1,253
SNARE-mediated membrane fusion
Chen, Y. A., & Scheller, R. H. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35052017 · Cited by 1,133
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Self-citationHanson, P. I., Roth, R. A., Morisaki, H., Jahn, R., & Heuser, J. E. (1997) · Cell · doi:10.1016/s0092-8674(00)80512-7 · Cited by 797
SNARE Function Analyzed in Synaptobrevin/VAMP Knockout Mice
Schoch, S., Deák, F., Königstorfer, A., Mozhayeva, M. G., Sara, Y., Südhof, T. C., & Kavalali, E. T. (2001) · Science · doi:10.1126/science.1064335 · Cited by 664
Snares and Munc18 in synaptic vesicle fusion
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Cited by
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SNAREs — engines for membrane fusion
Jahn, R., & Scheller, R. H. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2002 · Cited by 2,635
Expansion of the eukaryotic proteome by alternative splicing
Nilsen, T. W., & Graveley, B. R. (2010) · Nature · doi:10.1038/nature08909 · Cited by 2,270
Multiple Roles of Calcium Ions in the Regulation of Neurotransmitter Release
Neher, E., & Sakaba, T. (2008) · Neuron · doi:10.1016/j.neuron.2008.08.019 · Cited by 966
Self-citationPancreatic β-Cell Electrical Activity and Insulin Secretion: Of Mice and Men
Rorsman, P., & Ashcroft, F. M. (2018) · Physiological Reviews · doi:10.1152/physrev.00008.2017 · Cited by 793
Methods for the detection and analysis of protein–protein interactions
Berggård, T., Linse, S. S., & James, P. (2007) · PROTEOMICS · doi:10.1002/pmic.200700131 · Cited by 714
Metadata
- Authors
- Sørensen, J. B., Nagy, G., Varoqueaux, F., Nehring, R. B., Brose, N., Wilson, M. C., & Neher, E.
- Affiliations
- Max Planck Institute for Biophysical Chemistry (DE)
- Max Planck Institute of Experimental Medicine (DE)
- University of New Mexico (US)
- Corresponding author
- Sørensen, Jakob B.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2003-07
- Volume
- 114
- Issue
- 1
- Pages
- 75-86
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2137163623
- Cited by
- 364
- References
- 41
- Citations by year
- 2026: 1 · 2025: 8 · 2024: 4 · 2023: 4 · 2022: 9 · 2021: 12 · 2020: 11 · 2019: 11 · 2018: 13 · 2017: 12 · 2016: 14 · 2015: 17 · 2014: 13 · 2013: 13 · 2012: 11
- FWCI
- 9.50
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 3669 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Max Planck Institute for Plasma Physics (submittedVersion)
- GRO (submittedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion)
- Funders
- International Max Planck Research School for Environmental, Cellular and Molecular Microbiology
- Deutsche Forschungsgemeinschaft (SFB523)
- National Institutes of Health
- National Institute of Mental Health (MH 4-8989, R01MH048989)
- 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
- SNAP-25, SNAP23, SNARE complex, chromaffin cells, neuroexocytosis, calcium-triggered exocytosis, vesicle docking, vesicle fusion, fusion pore, splice variants
- MeSH terms
- Animals, Calcium, Carrier Proteins, Exocytosis, Fetus, Membrane Fusion, Membrane Proteins, Nerve Tissue Proteins, Neurosecretion, Neurosecretory Systems, Phenotype, Alternative Splicing, Mice, Knockout, Chromaffin Cells, Calcium Signaling, Secretory Vesicles, Qb-SNARE Proteins, Qc-SNARE Proteins, Synaptosomal-Associated Protein 25, Mice
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