RIM Binding Proteins (RBPs) Couple Rab3-Interacting Molecules (RIMs) to Voltage-Gated Ca2+ Channels
Open accessAbstract
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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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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Functional interaction of the active zone proteins Munc13-1 and RIM1 in synaptic vesicle priming
Betz, A., Thakur, P., Junge, H. J., Ashery, U., Rhee, J.-S., Scheuss, V., Rosenmund, C., Rettig, J., & Brose, N. (2001) · Neuron · doi:10.1016/s0896-6273(01)00272-0 · Cited by 425 · see citing works
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Südhof, T. C. (2012) · Neuron · doi:10.1016/j.neuron.2012.06.012 · Cited by 1,062 · see citing works
Calcium Channel Regulation and Presynaptic Plasticity
Catterall, W. A., & Few, A. P. (2008) · Neuron · doi:10.1016/j.neuron.2008.09.005 · Cited by 647 · see citing works
Nanodomain coupling between Ca2+ channels and sensors of exocytosis at fast mammalian synapses
Eggermann, E., Bucurenciu, I., Goswami, S. P., & Jonas, P. (2012) · Nature Reviews Neuroscience · doi:10.1038/nrn3125 · Cited by 500 · see citing works
RIM Proteins Activate Vesicle Priming by Reversing Autoinhibitory Homodimerization of Munc13
Deng, L., Kaeser, P. S., Xu, W., & Südhof, T. C. (2011) · Neuron · doi:10.1016/j.neuron.2011.01.005 · Cited by 287 · see citing works
Corominas, R., Yang, X., Lin, G. N., Kang, S., Shen, Y., Ghamsari, L., Broly, M., Rodriguez, M., Tam, S., Wanamaker, S. A., et al. (2014) · Nature Communications · doi:10.1038/ncomms4650 · Cited by 140 · see citing works
RIM genes differentially contribute to organizing presynaptic release sites
Kaeser, P. S., Deng, L., Fan, M., & Südhof, T. C. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1209318109 · Cited by 115 · see citing works
Minireview: How Peptide Hormone Vesicles Are Transported to the Secretion Site for Exocytosis
Park, J. J., & Loh, Y. P. (2008) · Molecular Endocrinology · doi:10.1210/me.2008-0209 · Cited by 81 · see citing works
Molecular and functional architecture of striatal dopamine release sites
Banerjee, A., Imig, C., Balakrishnan, K., Kershberg, L., Lipstein, N., Uronen, R.-L., Wang, J., Cai, X., Benseler, F., Rhee, J. S., et al. (2022) · Neuron · doi:10.1016/j.neuron.2021.10.028 · Cited by 58 · see citing works
Disentangling the roles of RIM and Munc13 in synaptic vesicle localization and neurotransmission
Zarebidaki, F., Camacho, M., Brockmann, M. M., Trimbuch, T., Herman, M. A., & Rosenmund, C. (2020) · The Journal of Neuroscience · doi:10.1523/jneurosci.1922-20.2020 · Cited by 37 · see citing works
Emperador-Melero, J., Andersen, J. W., Metzbower, S. R., Levy, A. D., Dharmasri, P. A., de Nola, G., Blanpied, T. A., & Kaeser, P. S. (2024) · Nature Neuroscience · doi:10.1038/s41593-024-01720-5 · Cited by 27 · see citing works
Ultrastructural analysis of wild-type and RIM1α knockout active zones in a large cortical synapse
Lichter, K., Paul, M. M., Pauli, M., Schoch, S., Kollmannsberger, P., Stigloher, C., Heckmann, M., & Sirén, A.-L. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111382 · Cited by 15 · see citing works
- 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)
- PMC
- PMC2151925
- 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
- bronze
- doi.org
- Licence
- 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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