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The RIM/NIM Family of Neuronal C2 Domain Proteins
Open accessAbstract
RIM1 is a putative effector protein for Rab3s, synaptic GTP-binding proteins. RIM1 is localized close to the active zone at the synapse, where it interacts in a GTP-dependent manner with Rab3 located on synaptic vesicles. We now describe a second RIM protein, called RIM2, that is highly homologous to RIM1 and also expressed primarily in brain. Like RIM1, RIM2 contains an N-terminal zinc finger domain that binds to Rab3 as a function of GTP, a central PDZ domain, and two C-terminal C(2) domains that are separated by long alternatively spliced sequences. Unexpectedly, the 3'-end of the RIM2 gene produces an independent mRNA that encodes a smaller protein referred as NIM2. NIM2 is composed of a unique N-terminal sequence followed by the C-terminal part of RIM2. Data bank searches identified a third RIM/NIM-related gene, which encodes a NIM isoform referred to as NIM3; no RIM transcript from this gene was detected. To test if NIMs, like RIMs, may function in secretion, we investigated the effect of NIM3 on calcium-triggered exocytosis in PC12 cells. NIM3 induced a dramatic increase in calcium-evoked exocytosis (50%), with no significant effect on base-line release, suggesting that NIMs, like RIMs, regulate exocytosis The combination of conserved and variable sequences in RIMs and NIMs indicates that the individual domains of these proteins provide binding sites for interacting molecules during exocytosis, as shown for the zinc finger domain of RIM, which binds to GTP-bound Rab3s.…
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“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 Wang et al., 2000
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Sorted by citations
Südhof, T. C. (2004) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.26.041002.131412 · Cited by 2,491
“…active zone (reviewed in Dresbach et al. 2001, Lonart, 2002; see Figure 5): Munc13s (Munc13-1, -2, and -3; Brose et al. 1995) and RIMs (Rab3- interacting molecules) (RIM1α, 2α/β/γ , 3γ , and 4γ ; Wang et al. 1997a, 2000; Wang & Südhof 2003) are multidomain proteins that interact with each other and”
InfluentialSelf-citationNeurotransmitter Release: The Last Millisecond in the Life of a Synaptic Vesicle
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“RIM and the RIM-interacting molecule RIM-BP (Wang et al., 2000) both bind to Ca2+ channels in addition to binding to each other (Kaeser et al., 2011).”
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Self-citationRIM proteins tether Ca2+ channels to presynaptic active zones via a direct PDZ-domain interaction
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Self-citationRIM1α forms a protein scaffold for regulating neurotransmitter release at the active zone
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Metadata
- Authors
- Wang, Y., Sugita, S., & Südhof, T. C.
- Affiliations
- Howard Hughes Medical Institute (US)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2000-06
- Volume
- 275
- Issue
- 26
- Pages
- 20033-20044
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2000501974
- Cited by
- 243
- References
- 42
- Citations by year
- 2026: 2 · 2025: 2 · 2024: 4 · 2023: 11 · 2022: 9 · 2021: 5 · 2020: 9 · 2019: 6 · 2018: 8 · 2017: 7 · 2016: 5 · 2015: 9 · 2014: 9 · 2013: 11 · 2012: 11
- FWCI
- 5.32
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- 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
- RIM1, C2 domain proteins, Rab3, synaptic vesicle exocytosis, calcium-triggered exocytosis, synaptic active zone, zinc finger, PDZ domain, alternative splicing, Src homology 3 domain, fibronectin type III domain, protein-protein interaction
- MeSH terms
- Rabphilin-3A, Amino Acid Sequence, Animals, Brain, Carrier Proteins, Chromatography, Affinity, Cloning, Molecular, DNA-Binding Proteins, Exocytosis, Fungal Proteins, Glutathione Transferase, Humans, Molecular Sequence Data, Nerve Tissue Proteins, Nuclear Proteins, Polymorphism, Genetic, Recombinant Fusion Proteins, Tissue Distribution, Transfection, PC12 Cells, Sequence Homology, Amino Acid, Alternative Splicing, Sequence Analysis, DNA, Protein Structure, Tertiary, DNA, Complementary, src Homology Domains, COS Cells, rab GTP-Binding Proteins, rab3 GTP-Binding Proteins, Two-Hybrid System Techniques, Membrane Transport Proteins, Vesicular Transport Proteins, Adaptor Proteins, Signal Transducing, Rats
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