Cited by 309Cellular transport and secretionIon channel regulation and functionNeuroscience and Neuropharmacology Research

RIM Binding Proteins (RBPs) Couple Rab3-Interacting Molecules (RIMs) to Voltage-Gated Ca2+ Channels

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Hibino, H., Pironkova, R., Onwumere, O., Vologodskaia, M., Hudspeth, A.J., Lesage, F.·2002·Neuron

Abstract

Ca(2+) influx through voltage-gated channels initiates the exocytotic fusion of synaptic vesicles to the plasma membrane. Here we show that RIM binding proteins (RBPs), which associate with Ca(2+) channels in hair cells, photoreceptors, and neurons, interact with alpha(1D) (L type) and alpha(1B) (N type) Ca(2+) channel subunits. RBPs contain three Src homology 3 domains that bind to proline-rich motifs in alpha(1) subunits and Rab3-interacting molecules (RIMs). Overexpression in PC12 cells of fusion proteins that suppress the interactions of RBPs with RIMs and alpha(1) augments the exocytosis triggered by depolarization. RBPs may regulate the strength of synaptic transmission by creating a functional link between the synaptic-vesicle tethering apparatus, which includes RIMs and Rab3, and the fusion machinery, which includes Ca(2+) channels and the SNARE complex.

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Crossref · 10.1016/s0896-6273(02)00667-0

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  • RIM-BPs bind nonsynaptic L-type Ca2+ channels as well as synaptic N- and P/Q-type Ca2+ channels.

    “However, the initial problem with this hypothesis was that RIM-BPs bind nonsynaptic L-type Ca2+ channels as well as synaptic N- and P/Q-type Ca2+ channels and thus could not account for the specific recruitment of N- and P/Q-type Ca2+ channels to active zones (Hibino et al., 2002).”

    From The Presynaptic Active Zone (2012) · cites this paper as Hibino et al., 2002

  • RIM-BPs bind to RIMs and to N-, P/Q-, and L-type Ca2+ channels.

    “However, the latter identification may be erroneous since subsequent studies showed that RIM-BPs are highly expressed only in brain and not peripherally and tightly bind to RIM (Wang et al., 2000) and to N-, P/Q-, and L-type Ca2+ channels (Hibino et al., 2002; Kaeser et al., 2011).”

    From The Presynaptic Active Zone (2012) · cites this paper as Hibino et al., 2002

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Authors
Hibino, H., Pironkova, R., Onwumere, O., Vologodskaia, M., Hudspeth, A. J., & Lesage, F.
Affiliations
Howard Hughes Medical Institute (US)
Corresponding author
Hudspeth, A.J.
Venue
Neuron
Publisher
Elsevier BV
Published
2002-04
Volume
34
Issue
3
Pages
411-423
ISSN
0896-6273 (ISSN-L)
OpenAlex
W2076227043
Cited by
309
References
1
Citations by year
2026: 3 · 2025: 6 · 2024: 16 · 2023: 22 · 2022: 15 · 2021: 17 · 2020: 16 · 2019: 14 · 2018: 20 · 2017: 16 · 2016: 14 · 2015: 16 · 2014: 11 · 2013: 14 · 2012: 12
FWCI
4.61
Type
journal article
Language
en
Open access
Locations
  • Neuron (publishedVersion)
  • PubMed (publishedVersion)
  • Europe PMC (PubMed Central) (acceptedVersion)
  • PubMed Central (acceptedVersion)
Funders
  • Howard Hughes Medical Institute
  • National Institute on Deafness and Other Communication Disorders (R01DC000241, DC-00317, F32DC000317)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion channel regulation and function
  • Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
Keywords
voltage-gated calcium channels, SH3 domain, proline-rich motif, synaptic vesicle exocytosis, synaptic vesicle tethering, SNARE complex, PC12 cells
MeSH terms
Animals, Brain, Carrier Proteins, Cell Fractionation, Chickens, Exocytosis, Hair Cells, Auditory, Models, Biological, Nerve Tissue Proteins, Neurons, Protein Binding, Recombinant Fusion Proteins, Retina, Synaptic Vesicles, PC12 Cells, Protein Structure, Tertiary, Protein Isoforms, Guanine Nucleotide Exchange Factors, Calcium Channels, L-Type, Two-Hybrid System Techniques, Calcium Channels, N-Type, Protein Subunits, Intracellular Signaling Peptides and Proteins, Rats

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