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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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“…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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Self-citationFunctional interaction of the active zone proteins Munc13-1 and RIM1 in synaptic vesicle priming
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“The N-terminal zinc fingers of RIM1 and its homolog RIM2 bind to Rab3A and other Rab3 In contrast to most other secretory processes, synaptic proteins in their GTP-bound state (Wang et al., 1997; neurotransmitter release is restricted to designated re- Ozaki et al., 2000; Wang et al., 2000).”
BackgroundBucan, M., Abrahams, B. S., Wang, K., Glessner, J. T., Herman, E. I., Sonnenblick, L. I., Alvarez Retuerto, A. I., Imielinski, M., Hadley, D., Bradfield, J. P., et al. (2009) · PLoS Genetics · doi:10.1371/journal.pgen.1000536 · Cited by 424
“Benzodiazapine receptor (peripheral) associated protein 1 (BZRAP1, alternatively referred to as RIMBP1), is an adaptor molecule thought to regulate synaptic transmission by linking vesicular release machinery to voltage gated Ca2+ channels [37].”
BackgroundMolecular dissection of the photoreceptor ribbon synapse
Dieck, S. T., Altrock, W. D., Kessels, M. M., Qualmann, B., Regus‐Leidig, H., Brauner, D., Fejtová, A., Bracko, O., Gundelfinger, E. D., & Brandstätter, J. H. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200408157 · Cited by 409
“The complete protein composition of the CAZ is not known to date, but it includes the proteins Munc13-1 (Brose et al., 1995), RIMs ( Wang et al., 1997, 2000 ), ERC/ CAST (Ohtsuka et al., 2002; Wang et al., 2002), Piccolo/Aczonin, and Bassoon (Cases-Langhoff et al., 1996; tom Dieck et al., 1998; Wang et al., 1999).”
BackgroundInfluentialRIM1α is required for presynaptic long-term potentiation
Castillo, P. E., Schoch, S., Schmitz, F., Südhof, T. C., & Malenka, R. C. (2002) · Nature · doi:10.1038/415327a · Cited by 389
Self-citationRIM determines Ca2+ channel density and vesicle docking at the presynaptic active zone
Han, Y., Kaeser, P. S., Südhof, T. C., & Schneggenburger, R. (2011) · Neuron · doi:10.1016/j.neuron.2010.12.014 · Cited by 354
“RIM proteins bind to multiple other presynaptic proteins—e.g., Rab3, Munc13’s, a-liprins, and RIM-binding proteins (RIM-BPs; Wang et al., 1997, 2000; Betz et al., 2001; Schoch et al., 2002; Dulubova et al., 2005).”
BackgroundSelf-citationRIM-Binding Protein, a Central Part of the Active Zone, Is Essential for Neurotransmitter Release
Liu, K. S. Y., Siebert, M., Mertel, S., Knoche, E., Wegener, S., Wichmann, C., Matkovic, T., Muhammad, K., Depner, H., Mettke, C., et al. (2011) · Science · doi:10.1126/science.1212991 · Cited by 306
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“…the localization of RIM1 in cultured neurons, but many proteins, including Rab3A (Wang et al., 1997), cAMP-GEFII (Ozaki et al., 2000), RIM-BPs (Wang et al., 2000), Munc13-1 (Betz et al., 2001), synaptotagmin (Coppola et al., 2001), Ca 2 channel (Coppola et al., 2001), and -liprin (Schoch et…”
BackgroundInfluentialSynaptic Vesicle ExocytosisPreprint
Südhof, T. C., & Rizo, J. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a005637 · Cited by 539
“The sequence between the two C2-domains includes a short prolinerich sequence that binds to RIM-BPs (RIMbinding proteins; Wang et al. 2000), whereas the second RIM C2-domain (the C2B-domain) binds to the active zone protein a-liprin (Schoch et al. 2002).”
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“In addition, Munc13s have an essential role in short-term synaptic plasticity (Rhee et al, 2002). a-RIMs are Rab3 effectors with two isoforms in mammals (RIM1a and RIM2a) (Wang et al, 1997, 2000; Wang and Südhof, 2003) that are homologues of C. elegans unc-10 (Koushika et al, 2001).”
BackgroundInfluentialSelf-citationRIM Proteins Activate Vesicle Priming by Reversing Autoinhibitory Homodimerization of Munc13
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“…Munc13 with synaptic vesicles via their N-terminal sequences and with other active zone proteins and Ca2+ channels via their C-terminal sequences (Wang et al., 1997, 2000, 2002; Betz et al., 2001; Schoch et al., 2002; Ohtsuka et al., 2002; Ko et al., 2003; Andrews-Zwilling et al., 2006; Kaeser…”
Self-citationRIM1 confers sustained activity and neurotransmitter vesicle anchoring to presynaptic Ca2+ channels
Kiyonaka, S., Wakamori, M., Miki, T., Uriu, Y., Nonaka, M., Bito, H., Beedle, A. M., Mori, E., Hara, Y., WAARD, M. M. D., et al. (2007) · Nature Neuroscience · doi:10.1038/nn1904 · Cited by 259
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“RIMS1 (regulating synaptic membrane exocytosis 1) is a RAB3A-interacting protein (Wang et al., 2000), and RAB3A is a synaptic-vesicle-associated protein involved in exocytosis.”
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“RIMs are localized close to the active zone at the synapse, where they interact in a GTP-dependent manner with Rab3s located on synaptic vesicles (Wang et al., 2000).”
RetractedSly1 binds to Golgi and ER syntaxins via a conserved N-terminal peptide motif.
Yamaguchi, T., Dulubova, I., Min, S.-W., Chen, X., Rizo, J., & Südhof, T. (2002) · Developmental Cell · doi:10.1016/s1534-5807(02)00125-9 · Cited by 223
Self-citationKuroda, T. S., Fukuda, M., Ariga, H., & Mikoshiba, K. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m112414200 · Cited by 211
RIM and RIM-BP Form Presynaptic Active-Zone-like Condensates via Phase Separation
Wu, X., Cai, Q., Shen, Z., Chen, X., Zeng, M., Du, S., & Zhang, M. (2019) · Molecular Cell · doi:10.1016/j.molcel.2018.12.007 · Cited by 242
“An isothermal titration calorimetry (ITC)-based binding assay confirmed the binding between PRM of RIM1a and all three SH3 domains of RIM-BP (Wang et al., 2000) and further showed that the third SH3 domain has the strongest binding affinity (Kd 1.”
BackgroundInfluentialDirect Interaction of the Rab3 Effector RIM with Ca2+Channels, SNAP-25, and Synaptotagmin*
Coppola, T., Magnin-Lüthi, S., Perret-Menoud, V., Gattesco, S., Schiavo, G., & Regazzi, R. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100929200 · Cited by 216
Wang, Y., Liu, X., Biederer, T., & Südhof, T. C. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.182532999 · Cited by 256
Self-citationThe presynaptic cytomatrix of brain synapses
Dresbach, T., Qualmann, B., Kessels, M. M., Garner, C. C., & Gundelfinger, E. D. (2001) · Cellular and Molecular Life Sciences · doi:10.1007/pl00000781 · Cited by 224
Ko, J., Na, M., Kim, S.-H., Lee, J.-R., & Kim, E. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m307561200 · Cited by 187
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Distinct Rab Binding Specificity of Rim1, Rim2, Rabphilin, and Noc2
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Presynaptic Mechanism Underlying cAMP-Dependent Synaptic Potentiation
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“An involvement of Rim2, which is also expressed in the neuronal system (Wang et al., 2000), remains as a possibility.”
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The Molecular Machinery of Neurotransmitter Release (Nobel Lecture)
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Self-citationMultiple Roles for the Active Zone Protein RIM1α in Late Stages of Neurotransmitter Release
Calakos, N., Schoch, S., Südhof, T. C., & Malenka, R. C. (2004) · Neuron · doi:10.1016/j.neuron.2004.05.014 · Cited by 155
Self-citationSensory Processing at Ribbon Synapses in the Retina and the Cochlea
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Bassoon Specifically Controls Presynaptic P/Q-type Ca2+ Channels via RIM-Binding Protein
Davydova, D., Marini, C., King, C., Klueva, J., Bischof, F., Romorini, S., Montenegro‐Venegas, C., Heine, M., Schneider, R., Schröder, M. S., et al. (2014) · Neuron · doi:10.1016/j.neuron.2014.02.012 · Cited by 181
Distinct Initial SNARE Configurations Underlying the Diversity of Exocytosis
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How to Make an Active Zone: Unexpected Universal Functional Redundancy between RIMs and RIM-BPs
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Self-citationMolecular mechanisms of active zone function
Rosenmund, C., Rettig, J., & Brose, N. (2003) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2003.09.011 · Cited by 144
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“, 2011) and with RIM-binding protein, another interactor of calcium channels (Wang et al., 2000; Hibino et al., 2002).”
BackgroundSensory Experience Engages Microglia to Shape Neural Connectivity through a Non-Phagocytic Mechanism
Cheadle, L., Rivera, S. A., Phelps, J. S., Ennis, K. A., Stevens, B., Burkly, L. C., Lee, W.-C. A., & Greenberg, M. E. (2020) · Neuron · doi:10.1016/j.neuron.2020.08.002 · Cited by 160
The molecular machinery of synaptic vesicle exocytosis
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Structural Basis for a Munc13–1 Homodimer to Munc13–1/RIM Heterodimer Switch
Lu, J., Machius, M., Dulubova, I., Dai, H., Südhof, T. C., Tomchick, D. R., & Rizo, J. (2006) · PLoS Biology · doi:10.1371/journal.pbio.0040192 · Cited by 132
“RIM2a [11,12].”
Self-citationRIM 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
Self-citationWang, Y., & Südhof, T. C. (2003) · Genomics · doi:10.1016/s0888-7543(02)00024-1 · Cited by 112
Self-citationRegus-Leidig, H., Dieck, S. T., Specht, D., Meyer, L., & Brandstätter, J. (2009) · The Journal of comparative neurology · doi:10.1002/cne.21915 · Cited by 108
“The mature CAZ of conventional chemical synapses is defined by a set of multidomain proteins that includes Munc13 (Brose et al., 1995), RIM (Wang et al., 1997, 2000), ERC/CAST (Ohtsuka et al., 2002; Wang et al., 2002), Piccolo/Aczonin (Cases-Langhoff et al., 1996; Wang et al., 1999), Bassoon (tom…”
BackgroundAssembly of Active Zone Precursor Vesicles
Dresbach, T., Torres, V. I., Wittenmayer, N., Altrock, W. D., Zamorano, P. L., Zuschratter, W., Nawrotzki, R., Ziv, N. E., Garner, C. C., & Gundelfinger, E. D. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508784200 · Cited by 107
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Liprin-α proteins: scaffold molecules for synapse maturation
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Liquid-Liquid Phase Separation in Neuronal Development and Synaptic Signaling
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“Finally, a PxxP sequence between the two C2-domains of RIM1 binds to RIMBPs (Wang et al., 2000), and the N-terminal region of RIM1 binds to 14-3-3 proteins (Sun et al., 2003; Simsek-Duran et al., 2004; Kaeser et al., 2008).”
BackgroundSelf-citationRIM Promotes Calcium Channel Accumulation at Active Zones of theDrosophilaNeuromuscular Junction
Graf, E. R., Valakh, V., Wright, C. M., Wu, C., Liu, Z., Zhang, Y., & DiAntonio, A. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.0965-12.2012 · Cited by 101
“, 2011) but also interacting with each other and several other components to form the active zone cytomatrix (Wang et al., 2000; Betz et al., 2001; Coppola et al., 2001; Ohtsuka et al., 2002; Schoch et al., 2002; Wang et al., 2002; Deken et al., 2005; Dulubova et al., 2005).”
BackgroundInfluentialRIM function in short- and long-term synaptic plasticity
Kaeser, P. S., & Südhof, T. C. (2005) · Biochemical Society Transactions · doi:10.1042/bst20051345 · Cited by 82
Self-citationVoltage-Gated Calcium Channels: Key Players in Sensory Coding in the Retina and the Inner Ear
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RIM-BP3 is a manchette-associated protein essential for spermiogenesis
Zhou, J., Du, Y.-R., Qin, W., Hu, Y.-G., Huang, Y.-N., Bao, L., Han, D., Mansouri, A., & Xu, G.-L. (2009) · Development · doi:10.1242/dev.030858 · Cited by 83
“These genes are involved in the regulation of acrosome biogenesis (Hrb, Gopc and Csnk2a2) (Escalier et al., 2003; Kang-Decker et al., 2001; Yao et al., 2002), tail formation (Tektin-t, Vdac3, Sepp1, Akap4 and Spag6) (Olson et al., 2005; Sampson et al., 2001; Sapiro et al., 2002; Shirohzu et al., 2002; Tanaka et al., 2…”
Comprehensive genomics linking between neural development and cancer: neuroblastoma as a model.
Nakagawara, A., & Ohira, M. (2004) · Cancer Letters · doi:10.1016/s0304-3835(03)00457-9 · Cited by 81
“Nbla00697) [65], RAB3 efffector protein RIM1 (Nbla00761) [ 66 ], cell recognition molecule”
Synaptotagmin-like protein 5: a novel Rab27A effector with C-terminal tandem C2 domains
Kuroda, T. S., Fukuda, M., Ariga, H., & Mikoshiba, K. (2002) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)00320-0 · Cited by 82
Specific Regulation of IRS-2 Expression by Glucose in Rat Primary Pancreatic Islet β-Cells*
Lingohr, M. K., Briaud, I., Dickson, L. M., McCuaig, J., Alárcon, C., Wicksteed, B., & Rhodes, C. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600356200 · Cited by 79
Molecular Machines Regulating the Release Probability of Synaptic Vesicles at the Active Zone
Körber, C., & Kuner, T. (2016) · Frontiers in Synaptic Neuroscience · doi:10.3389/fnsyn.2016.00005 · Cited by 77
“It has been shown that the increase in presynaptic calcium concentration during high frequency synaptic activity speeds-up the refilling of the RRP at the calyx of Held (Wang and Kaczmarek, 1998).”
BackgroundRIM proteins and their role in synapse function
Mittelstaedt, T., Álvarez‐Barón, E., & Schoch, S. (2010) · Biological Chemistry · doi:10.1515/bc.2010.064 · Cited by 82
“The RIM C2 domains do not contain the consensus calcium binding sites that have been defined in the Synaptotagmin C2 domains, and do not bind to phospholipids (Wang et al., 2000).”
BackgroundAsaba, N., Hanada, T., Takeuchi, A., & Chishti, A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210362200 · Cited by 69
Modulation of Cav1.3 Ca2+ channel gating by Rab3 interacting molecule
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Regulation of Arabidopsis COPINE 1 Gene Expression in Response to Pathogens and Abiotic Stimuli1
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“C2 domain-containing proteins include protein kinase C (Azzi et al., 1992), phospholipase C (Essen et al., 1996), synaptotagmin (Brose et al., 1995), and rabphilin (Wang et al., 2000).”
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“RIMs are found in the active zone of presynaptic nerve terminals, the sites on the plasma membrane where synaptic vesicle exocytosis occurs (Wang et al., 2000).”
BackgroundWang, X., Hu, B., Zimmermann, B., & Kilimann, M. W. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103337200 · Cited by 59
Hamanaka, Y., & Meinertzhagen, I. A. (2009) · The Journal of Comparative Neurology · doi:10.1002/cne.22268 · Cited by 56
“Although knowledge of the complete protein composition of the CAZ remains incomplete, the list includes: Munc13-1 (Brose et al., 1995), RIMs (Wang et al., 1997, 2000), ERC/ CAST (Ohtsuka et al., 2002; Wang et al., 2002), Piccolo/ Aczonin, and Bassoon (Cases-Langhoff et al., 1996; tom Dieck et al.,…”
BackgroundGerber, S. H., Garcia, J. M., Rizo, J., & Südhof, T. (2001) · EMBO Journal · doi:10.1093/emboj/20.7.1605 · Cited by 56
Self-citationSynapse development and maturation at the drosophila neuromuscular junction
Chou, V., Johnson, S. A., & Vactor, D. V. (2020) · Neural Development · doi:10.1186/s13064-020-00147-5 · Cited by 73
Molecular Organization and Assembly of the Presynaptic Active Zone of Neurotransmitter Release
Fejtová, A., & Gundelfinger, E. D. (2006) · Results and problems in cell differentiation · doi:10.1007/400_012 · Cited by 51
“The diversity of RIM family members is even increased by alternative splicing of α and β isoforms ( Wang et al. 2000; Wang and Sudhof 2003).”
BackgroundInfluentialMolecular mechanisms of synaptogenesis
Qi, C., Luo, L.-D., Feng, I., & Ma, S. (2022) · Frontiers in Synaptic Neuroscience · doi:10.3389/fnsyn.2022.939793 · Cited by 54
“…domains, the active zone protein RIM (Rab3 Interacting Molecules) and its interaction partners such as RIM-BP, ELKS, and CAST were identified (Wang et al., 1997, 2000, 2002) [sub-cellular fractionation of mammals’ synaptic fraction also independently discovered CAST (Ohtsuka et al., 2002)].”
BackgroundSaw, N. M. N., Kang, S.-Y. A., Parsaud, L., Han, G. A., Jiang, T., Grzegorczyk, K., Surkont, M., Sun‐Wada, G., Wada, Y., Li, L., et al. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-02-0155 · Cited by 50
“…315– Volume 22 September 15, 2011 Voa1/Voa2 in vesicular acidification | 3407 in K-glutamate buffer (20 mM HEPES, pH 7.1, 140 mM potassium glutamate, 2 mM EGTA, 1 mM MgCl2), and mechanically permeabilized with a ball homogenizer (Wang et al., 2000, 2004a; Fujita et al., 2007; Li et al., 2007).”
MethodInfluentialSelf-citationWater channels and zymogen granules in salivary glands.
Ishikawa, Y., Cho, G., Yuan, Z.-F., Skowroński, M., Pan, Y., & Ishida, H. (2006) · Journal of Pharmacological Sciences · doi:10.1254/jphs.crj06007x · Cited by 53
Structure and evolution of RIM-BP genes: Identification of a novel family member
Mittelstaedt, T., & Schoch, S. (2007) · Gene · doi:10.1016/j.gene.2007.08.004 · Cited by 57
“RIM-BPs display structures typical of adaptor proteins and have been shown to interact with the active zone proteins RIM1 and RIM2 as well as with different α-subunits of voltage-gated calcium channels (Wang et al., 2000; Hibino et al., 2002).”
BackgroundInfluentialRab3D: a regulator of exocytosis in non-neuronal cells.
Millar, A., Pavios, N. J., Xu, J., & Zheng, M.-H. (2002) · Histology and Histopathology · doi:10.14670/hh-17.929 · Cited by 50
Variants in several genomic regions associated with asperger disorder
Salyakina, D., Ma, D. Q., Jaworski, J. M., Konidari, I., Whitehead, P. L., Henson, R., Martinez, D. M., Robinson, J. L., Sacharow, S. J., Wright, H. H., et al. (2010) · Autism Research · doi:10.1002/aur.158 · Cited by 44
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RIM1: an edge for presynaptic plasticity
Lónárt, G. (2002) · Trends in Neurosciences · doi:10.1016/s0166-2236(02)02193-8 · Cited by 51
Ellencrona, K., Syed, A., & Johansson, M. (2009) · Biological Chemistry · doi:10.1515/bc.2009.041 · Cited by 53
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“3 (Y. Wang et al., 2000; Hibino et al., 2002; Kaeser et al., 2011; Davydova et al., 2014).”
Differential signaling in presynaptic neurotransmitter release
Ghijsen, W. E. J. M., & Leenders, A. G. M. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-004-4525-0 · Cited by 50
Serano, J. M., & Rubin, G. M. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1835727100 · Cited by 43
Solution Structure of the RIM1α PDZ Domain in Complex with an ELKS1b C-terminal Peptide
Lu, J., Li, H., Wang, Y., Südhof, T. C., & Rizo, J. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.07.047 · Cited by 40
Self-citationRetinitis Pigmentosa and Allied Disorders
Gregory-Evans, K., Pennesi, M. E., & Weleber, R. G. (2012) · Elsevier eBooks · doi:10.1016/b978-1-4557-0737-9.00040-0 · Cited by 112
Khanna, R., Li, Q., Sun, L., Collins, T. J., & Stanley, E. F. (2006) · Neuroscience · doi:10.1016/j.neuroscience.2006.04.053 · Cited by 37
Ortega, J. M., Genç, Ö., & Davis, G. W. (2018) · eLife · doi:10.7554/elife.40385 · Cited by 40
Coupling the Structural and Functional Assembly of Synaptic Release Sites
Ghelani, T., & Sigrist, S. J. (2018) · Frontiers in Neuroanatomy · doi:10.3389/fnana.2018.00081 · Cited by 40
Maturation of Synaptic Contacts in Differentiating Neural Stem Cells
Liebau, S., Vaida, B., Storch, A., & Boeckers, T. M. (2007) · Stem Cells · doi:10.1634/stemcells.2006-0823 · Cited by 34
Enrichment of integral membrane proteins from small amounts of brain tissue
Schindler, J., Jung, S.-Y., Niedner‐Schatteburg, G., Friauf, E., & Nothwang, H. G. (2006) · Journal of Neural Transmission · doi:10.1007/s00702-006-0508-4 · Cited by 36
“Another identified protein was the Rab3-interacting protein 2 (RIMS2) which is involved in synaptic release (Wang et al., 2000; Graham et al., 2004; Sudhof, 2004).”
Wang, J., Lv, X., Wu, Y., Xu, T., Jiao, M., Yang, R., Li, X., Chen, M., Yan, Y.-G., Chen, C., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-04672-0 · Cited by 38
Voltage-gated calcium channels function as Ca2+-activated signaling receptors
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“Most of the well-characterized VWA domains are found in celladhesion and extracellular-matrix (ECM) proteins, such as integrin b subunits, hemicentin and matrilins ( Tuckwell 1999; Whittaker and Hynes 2002).”
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Rab3a Binding and Secretion-enhancing Domains in Rim1 Are Separate and Unique
Sun, L., Bittner, M. A., & Holz, R. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m011110200 · Cited by 33
Development and maintenance of vision’s first synapse
Burger, C. A., Jiang, D., Mackin, R. D., & Samuel, M. A. (2021) · Developmental Biology · doi:10.1016/j.ydbio.2021.04.001 · Cited by 41
Cell entry machines: a common theme in nature?
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“1 ); and they involve additional factors, such as the exocyst multi-subunit protein docking complex, microtubules and the recruitment of tethering proteins through Rab GTPases (such as Rab3A”
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Molecular organization of excitatory chemical synapses in the mammalian brain
Gundelfinger, E. D., & Dieck, S. T. (2000) · Die Naturwissenschaften · doi:10.1007/s001140050770 · Cited by 28
“RIM1 and RIM2 as well as shorter RIM isoforms containing only the Cterminal C2 domain (named NIM2 and NIM3) can influence Ca2c-evoked exocytosis from PC12 cells and are therefore likely to be involved in the regulation of neurotransmitter release (Wang et al. 1997, 2000).”
BackgroundInfluentialLai, C., Ho, Y., Hsieh, M., Wang, H.-H., Cheng, J., Chau, Y., & Peng, H. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.1732-16.2016 · Cited by 32
“RIM1 , the major isoform of mammalian RIM families, was shown to bind with synaptic proteins to mediate vesicle release (Wang et al., 1997, 2000; Kaeser and Südhof, 2005).”
Background
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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