RIM-BP2 primes synaptic vesicles via recruitment of Munc13-1 at hippocampal mossy fiber synapses


  • M.M. Brockmann
  • M. Maglione
  • C.G. Willmes
  • A. Stumpf
  • B.A. Bouazza
  • L.M. Velasquez
  • M.K. Grauel
  • P. Beed
  • M. Lehmann
  • N. Gimber
  • J. Schmoranzer
  • S.J. Sigrist
  • C. Rosenmund
  • D. Schmitz


  • eLife


  • eLife 8: e43243


  • 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 Ca(2+)-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.