1. RIM-BP2 primes synaptic vesicles via recruitment of Munc13-1 at hippocampal mossy fiber synapses.
- Author
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Brockmann MM, Maglione M, Willmes CG, Stumpf A, Bouazza BA, Velasquez LM, Grauel MK, Beed P, Lehmann M, Gimber N, Schmoranzer J, Sigrist SJ, Rosenmund C, and Schmitz D
- Subjects
- Animals, Mice, Neurotransmitter Agents metabolism, Intracellular Signaling Peptides and Proteins metabolism, Mossy Fibers, Hippocampal metabolism, Nerve Tissue Proteins metabolism, Neurons metabolism, Synaptic Vesicles metabolism
- Abstract
All synapses require fusion-competent vesicles and coordinated Ca
2+ -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., Competing Interests: MB, MM, CW, AS, BB, LV, MG, PB, ML, NG, JS, SS, CR, DS No competing interests declared, (© 2019, Brockmann et al.)- Published
- 2019
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