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Differential expression of two novel Munc13 proteins in rat brain
Open accessAbstract
Munc13-1, a mammalian homologue of Caenorhabditis elegans unc-13p, is a presynaptic phorbol ester receptor that enhances neurotransmitter release. In the present study we analysed the regional, cellular and subcellular expression patterns in rat of two novel Munc13 proteins, Munc13-2 and Munc13-3. We demonstrate by hybridization in situ that Munc13-1 mRNA is expressed throughout the brain, whereas Munc13-2 mRNA is preferentially present in rostral brain regions, and Munc13-3 mRNA in caudal areas. In an analysis of subcellular brain fractions with isoform-specific antibodies, we show that the novel Munc13 proteins are enriched in synapses. Immunocytochemical examination of rat cerebellar sections indicates that Munc13-3, like Munc13-1, is concentrated in presynaptic terminals. Our results characterize Munc13 proteins as a family of neuron-specific, synaptic molecules that bind to syntaxin, an essential mediator of neurotransmitter release. Munc13-2 and Munc13-3 are expressed in a complementary fashion and might act in concert with Munc13-1 to modulate neurotransmitter release.
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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 [40]
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“After Munc13-1, the second-most abundant isoform expressed at MFB synapses is bMunc13-2 [40,42,77].”
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 [40]
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“In this context, it is interesting that forskolin changes only the localization of Munc13-1 but not bMunc13-2, which lacks C2A domain and is thought to prime vesicles independently of RIM [40,96].”
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 [40]
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Metadata
- Authors
- AUGUSTIN, I., BETZ, A., HERRMANN, C., JO, T., & BROSE, N.
- Affiliations
- Max Planck Institute of Experimental Medicine (DE)
- Max Planck Institute for Biophysical Chemistry (DE)
- Max-Planck-Institut für biophysikalische Chemie, Abteilung Neurobiologie, Am Fassberg 11, D-37077 Göttingen, Germany
- Corresponding author
- AUGUSTIN, Iris
- BETZ, Andrea
- BROSE, Nils
- ORCID
- BROSE, Nils
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 1999-01-25
- Volume
- 337
- Issue
- 3
- Pages
- 363-371
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- PMC
- PMC1219986
- OpenAlex
- W2046553750
- Cited by
- 151
- References
- 29
- Citations by year
- 2026: 3 · 2025: 4 · 2024: 3 · 2023: 4 · 2022: 8 · 2021: 5 · 2020: 6 · 2019: 6 · 2018: 6 · 2017: 9 · 2016: 3 · 2015: 4 · 2014: 5 · 2013: 5 · 2012: 5
- FWCI
- 2.48
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Biochemical Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- GRO (submittedVersion)
- Funders
- Deutsche Forschungsgemeinschaft (SFB406/A1)
- 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
- Munc13-1, presynaptic proteins, neurotransmitter release, syntaxin, presynaptic terminals, cerebellum, brain regional expression, subcellular localization, synapses, rat brain
- MeSH terms
- Amino Acid Sequence, Animals, Brain, Male, Membrane Proteins, Molecular Sequence Data, Nerve Tissue Proteins, Organ Specificity, RNA, Messenger, Subcellular Fractions, Rats, Wistar, In Situ Hybridization, Intracellular Signaling Peptides and Proteins, Qa-SNARE Proteins, Mice, Rats
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