Rim is a putative Rab3 effector in regulating synaptic-vesicle fusion
Abstract
Rab3 is a neuronal GTP-binding protein that regulates fusion of synaptic vesicles and is essential for long-term potentiation of hippocampal mossy fibre synapses. More than thirty Rab GTP-binding proteins are known to function in diverse membrane transport pathways, although their mechanisms of action are unclear. We have now identified a putative Rab3-effector protein called Rim. Rim is composed of an amino-terminal zinc-finger motif and carboxy-terminal PDZ and C2 domains. It binds only to GTP (but not to GDP)-complexed Rab3, and interacts with no other Rab protein tested. There is enrichment of Rab3 and Rim in neurons, where they have complementary distributions. Rab3 is found only on synaptic vesicles, whereas Rim is localized to presynaptic active zones in conventional synapses, and to presynaptic ribbons in ribbon synapses. Transfection of PC12 cells with the amino-terminal domains of Rim greatly enhances regulated exocytosis in a Rab3-dependent manner. We propose that Rim serves as a Rab3-dependent regulator of synaptic-vesicle fusion by forming a GTP-dependent complex between synaptic plasma membranes and docked synaptic vesicles.
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RIMs contain five identifiable domains: an N-terminal composite domain consisting of a zinc finger surrounded by α helices, a central PDZ domain, two C-terminal C2 domains that do not bind Ca2+, and a conserved proline-rich sequence in the linker between the C2 domains.
“RIMs (for Rab3-interacting molecules; Wang et al., 1997) contain five identifiable domains (Figure 2): an N-terminal composite domain consisting of a zinc finger surrounded by α helices, a central PDZ domain, two C-terminal C2 domains that different from classical C2 domains do not bind Ca2+, and a conserved proline-rich sequence in the linker sequence between the C2 domains (Wang and Südhof, 2003”
From The Presynaptic Active Zone (2012) · cites this paper as Wang et al., 1997
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References 32 · Cited by 684
- Authors
- Wang, Y., Okamoto, M., Schmitz, F., Hofmann, K., & Südhof, T. C.
- Affiliations
- The University of Texas Southwestern Medical Center (US)
- Howard Hughes Medical Institute (US)
- Max Planck Society (DE)
- Corresponding author
- Südhof, Thomas C.
- Venue
- Nature
- Published
- 1997-08-07
- Volume
- 388
- Issue
- 6642
- Pages
- 593-598
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W1591639440
- Cited by
- 684
- References
- 32
- Citations by year
- 2026: 7 · 2025: 8 · 2024: 4 · 2023: 15 · 2022: 23 · 2021: 13 · 2020: 11 · 2019: 14 · 2018: 16 · 2017: 21 · 2016: 15 · 2015: 17 · 2014: 25 · 2013: 22 · 2012: 29
- FWCI
- 14.10
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- W. M. Keck Foundation
- Deutsche Forschungsgemeinschaft
- National Institutes of Health
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- RIM, Rab3, synaptic vesicle fusion, regulated exocytosis, active zone, ribbon synapses, PDZ domain, C2 domain, zinc finger, long-term potentiation, PC12 cells
- MeSH terms
- Rabphilin-3A, Amino Acid Sequence, Animals, Brain, Calcium, Exocytosis, Guanosine Triphosphate, Membrane Fusion, Molecular Sequence Data, Mutation, Nerve Tissue Proteins, Neurons, Recombinant Fusion Proteins, Retina, Saccharomyces cerevisiae, Spinal Cord, Subcellular Fractions, Synaptic Membranes, Synaptic Vesicles, Transfection, Zinc Fingers, PC12 Cells, Mice, Knockout, GTP-Binding Proteins, rab GTP-Binding Proteins, rab3 GTP-Binding Proteins, Vesicular Transport Proteins, Adaptor Proteins, Signal Transducing, Mice, Rats
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