Dendritic SNAREs add a new twist to the old neuron theory
Open accessAbstract
Dendritic exocytosis underpins a broad range of integrative and homeostatic synaptic functions. Emerging data highlight the essential role of SNAREs in trafficking and fusion of secretory organelles with release of peptides and neurotransmitters from dendrites. This Perspective analyzes recent evidence inferring axo-dendritic polarization of vesicular release machinery and pinpoints progress made with existing challenges in this rapidly progressing field of dendritic research. Interpreting the relation of new molecular data to physiological results on secretion from dendrites would greatly advance our understanding of this facet of neuronal mechanisms.
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SNAP-25 has recently been shown to facilitate the removal of kainate receptors (KARs) from the membrane surface.
“Moreover, SNAP-25 has recently been shown to facilitate the removal of kainate receptors (KARs), which are implicated in epileptogenesis, from the membrane surface (83, 90 -95).”
From Analysis of proteins that rapidly change upon mechanistic/mammalian target of rapamycin complex 1 (mTORC1) repression identifies parkinson protein 7 (PARK7) as a novel protein aberrantly expressed in tuberous sclerosis complex (TSC) (2016) · cites this paper as [83]
The section ‘Evidence for Specialization of Exocytotic Machinery for Dendritic Secretion’ discusses SNAP-25 localization and identifies SNAP-23 in dendritic fusion; it does not say SNAP-25 removes kainate receptors from the membrane. Searches for kainate receptors, receptor endocytosis, and epileptogenesis found no passage addressing the claimed effect. (LLM, conf=0.76)
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Cites
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The oxytocin receptor: from intracellular signaling to behavior
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“Consistent with the localization of Gap-43 and Snap-25 mRNAs in the dendrites, our findings show that GAP-43 and SNAP-25 proteins are present postsynaptically (82, 83).”
Background
- Authors
- Ovsepian, S. V., & Dolly, J. O.
- Affiliations
- Dublin City University (IE)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2011-11-11
- Volume
- 108
- Issue
- 48
- Pages
- 19113-19120
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC3228427
- OpenAlex
- W1986097748
- Cited by
- 50
- References
- 5
- Citations by year
- 2026: 1 · 2025: 2 · 2023: 4 · 2022: 2 · 2021: 2 · 2020: 5 · 2019: 2 · 2018: 6 · 2017: 3 · 2016: 6 · 2015: 5 · 2014: 3 · 2013: 5 · 2012: 4
- FWCI
- 0.33
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- 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
- SNARE proteins, neurotransmitter release, peptide release, synaptic integration
- MeSH terms
- Calcium, Dendrites, Membrane Fusion, Models, Biological, Neurons, Synapses, Cell Polarity, Transport Vesicles, SNARE Proteins
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