| Home > Publications Database > RIM-BP2 primes synaptic vesicles via recruitment of Munc13-1 at hippocampal mossy fiber synapses. |
| Journal Article | DZNE-2020-07883 |
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2019
eLife Sciences Publications
Cambridge
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Please use a persistent id in citations: doi:10.7554/eLife.43243
Abstract: All synapses require fusion-competent vesicles and coordinated Ca2+-secretion coupling for neurotransmission, yet functional and anatomical properties are diverse across different synapse types. We show that the presynaptic protein RIM-BP2 has diversified functions in neurotransmitter release at different central murine synapses and thus contributes to synaptic diversity. At hippocampal pyramidal CA3-CA1 synapses, RIM-BP2 loss has a mild effect on neurotransmitter release, by only regulating Ca2+-secretion coupling. However, at hippocampal mossy fiber synapses, RIM-BP2 has a substantial impact on neurotransmitter release by promoting vesicle docking/priming and vesicular release probability via stabilization of Munc13-1 at the active zone. We suggest that differences in the active zone organization may dictate the role a protein plays in synaptic transmission and that differences in active zone architecture is a major determinant factor in the functional diversity of synapses.
Keyword(s): Intracellular Signaling Peptides and Proteins: metabolism (MeSH) ; Animals (MeSH) ; Mice (MeSH) ; Mossy Fibers, Hippocampal: metabolism (MeSH) ; Nerve Tissue Proteins: metabolism (MeSH) ; Neurons: metabolism (MeSH) ; Neurotransmitter Agents: metabolism (MeSH) ; Synaptic Vesicles: metabolism (MeSH) ; Nerve Tissue Proteins ; Neurotransmitter Agents ; Unc13a protein, mouse
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