The DOI matches its Crossref record, with a small difference in title or year; 38 of the 42 references it cites were found in a registry or an index.
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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“Benzodiazapine receptor associated protein 1 (TSPOAP1), is another adaptor molecule interacting with Ca2+ channels to regulate synaptic transmission (Wang et al., 2000b).”
BackgroundMaschi, D., & Klyachko, V. A. (2020) · eLife · doi:10.7554/elife.55210 · Cited by 30
“, 2016), which have been suggested to control the recruitment and clustering of VGCCs at the AZ via the RIM binding protein RIM-BP (Davydova et al., 2014; Hibino et al., 2002; Wang et al., 2000).”
BackgroundZhang, L., Wang, T., Wright, A. F., Suri, M., Schwartz, C. E., Stevenson, R. E., & Valle, D. L. (2006) · American Journal of Medical Genetics Part A · doi:10.1002/ajmg.a.31080 · Cited by 24
“Most notablyNIM3, which is expressed in the central but not peripheral nervous system and belongs to a small family of proteins that interactwith Rab proteins in synaptic vesicles [Wang et al., 2000].”
BackgroundFukuda, M. (2004) · Genes to Cells · doi:10.1111/j.1365-2443.2004.00767.x · Cited by 22
Regulation of Voltage-Gated Calcium Channels by Synaptic Proteins
Weiss, N., & Zamponi, G. W. (2012) · Advances in experimental medicine and biology · doi:10.1007/978-94-007-2888-2_33 · Cited by 33
Juranek, J. K., Mukherjee, K., Rickmann, M., Martens, H., Całka, J., Südhof, T. C., & Jahn, R. (2006) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2006.05183.x · Cited by 28
“RIMs represent a family of multidomain proteins that bind to Munc13 and Rab3a, a neuronal GTPase localized to synaptic vesicles (Wang et al., 2000) thus providing a direct link between synaptic vesicles and active zone constituents.”
BackgroundSelf-citationTorres, V. I., & Inestrosa, N. C. (2017) · Molecular Neurobiology · doi:10.1007/s12035-017-0661-9 · Cited by 29
Fan, F., Matsunaga, K., Wang, H., Ishizaki, R., Kobayashi, E., Kiyonari, H., Mukumoto, Y., Okunishi, K., & Izumi, T. (2017) · eLife · doi:10.7554/elife.26174 · Cited by 22
“We further show that exophilin-8 directly interacts with RIM-BP2, a binding protein to RIM (Wang et al., 2000), and that this complex formation is essential for both peripheral accumulation and efficient exocytosis of granules.”
BackgroundRegus‐Leidig, H., Dieck, S. T., & Brandstätter, J. H. (2010) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2009.12.006 · Cited by 29
“CAZ components include Piccolo/ Aczonin (Cases-Langhoff et al., 1996; Wang et al., 1999), Bassoon (tom Dieck et al., 1998), Munc13 (Brose et al., 1995), RIMs (Wang et al., 1997, 2000), ERC/CAST (Ohtsuka et al., 2002; Wang et al., 2002) and CtBP1 (tom Dieck et al., 2005).”
RIM-binding protein couples synaptic vesicle recruitment to release sites
Petzoldt, A. G., Götz, T., Driller, J. H., Lützkendorf, J., Reddy‐Alla, S., Matkovic, T., Liu, S., Knoche, E., Mertel, S., Ugorets, V., et al. (2020) · The Journal of Cell Biology · doi:10.1083/jcb.201902059 · Cited by 42
“RIM-BPs bind via their SH3-II/III domains to voltagegated Ca2+ channel α1 subunits (Hibino et al., 2002; Wang et al., 2000, 2002), with sequence and position of interaction motifs and domains highly similar between Drosophila and mammals (Siebert et al., 2015).”
BackgroundLRGUK1 is part of a multiprotein complex required for manchette function and male fertility
Okuda, H., DeBoer, K., O’Connor, A. E., Merriner, D. J., Jamsai, D., & O’Bryan, M. K. (2016) · The FASEB Journal · doi:10.1096/fj.201600909r · Cited by 30
Crystal Structure of the RIM2 C2A-Domain at 1.4 Å Resolution,
Dai, H., Tomchick, D. R., García, J., Südhof, T. C., Machius, M., & Rizo, J. (2005) · Biochemistry · doi:10.1021/bi0513608 · Cited by 21
“rich sequence between the two C2-domains binds to RIMbinding proteins (RIM-BPs) (17).”
BackgroundSelf-citationWeidenhofer, J., Scott, R. J., & Tooney, P. A. (2008) · Journal of Psychiatric Research · doi:10.1016/j.jpsychires.2008.04.001 · Cited by 24
Wu, S., Fan, J., Tang, F., Chen, L., Zhang, X., Xiao, D., & Li, X. (2023) · Frontiers in Neuroscience · doi:10.3389/fnins.2023.1123561 · Cited by 26
“Different RIM protein subtypes are expressed in the cerebrum, hippocampus, cerebellum, calyx synapses, photoreceptors, and spinal cord of rats and mice (Wang et al., 2000; Zanazzi and Matthews, 2009; Gandini and Felix, 2012).”
BackgroundMechanisms controlling the trafficking, localization, and abundance of presynaptic Ca2+ channels
Cunningham, K. L., & Littleton, J. T. (2023) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.1116729 · Cited by 25
Nanomachinery Organizing Release at Neuronal and Ribbon Synapses
Chakrabarti, R., & Wichmann, C. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20092147 · Cited by 22
Yang, Y., & Calakos, N. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.4285-09.2010 · Cited by 19
“RIM1 is an active zone scaffold protein that binds to many presynaptic proteins involved in neurotransmitter release and synapse formation (Wang et al., 1997, 2000, 2002; Zhen and Jin, 1999; Betz et al., 2001; Coppola et al., 2001; Wang et al., 2001; Ohtsuka et al., 2002; Schoch et al., 2002; Sun…”
BackgroundRBP2 stabilizes slow Cav1.3 Ca2+ channel inactivation properties of cochlear inner hair cells
Ortner, N., Pinggera, A., Hofer, N. T., Siller, A., Brandt, N., Raffeiner, A., Vilusic, K., Lang, I., Blum, K., Obermair, G., et al. (2019) · Pflügers Archiv: European Journal of Physiology · doi:10.1007/s00424-019-02338-4 · Cited by 21
Gandini, M. A., & Felix, R. (2011) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2011.12.011 · Cited by 21
Pushing synaptic vesicles over the RIM
Kaeser, P. S. (2011) · Cellular Logistics · doi:10.4161/cl.1.3.16429 · Cited by 27
Sons, M. S., & Plomp, J. J. (2006) · Brain Research · doi:10.1016/j.brainres.2006.03.055 · Cited by 20
Glutathione S-transferase pull-down assays using dehydrated immobilized glutathione resin.
Ren, L., Chang, E., Makky, K., Haas, A., Kaboord, B., & Qoronfleh, M. (2003) · Analytical Biochemistry · doi:10.1016/j.ab.2003.07.023 · Cited by 20
Expression profile and up-regulation of PRAX-1 mRNA by antidepressant treatment in the rat brain.
Chardenot, P., Roubert, C., Galiègue, S., Casellas, P., le Fur, G., Soubrié, P., & Oury-Donat, F. (2002) · Molecular Pharmacology · doi:10.1124/mol.62.6.1314 · Cited by 20
“Although the present studies thus point to a role for PRAX-1 in the treatment of depression, its cellular function remains unknown but might be related to that of RIM-BP1, a rat homolog of PRAX-1 (Wang et al., 2000).”
BackgroundCharacterization of rabphilin phosphorylation using phospho-specific antibodies.
Lónárt, G., & Südhof, T. (2001) · Neuropharmacology · doi:10.1016/s0028-3908(01)00126-5 · Cited by 20
Self-citationCutforth, T., & Harrison, C. (2002) · Trends in Neurosciences · doi:10.1016/s0166-2236(02)02187-2 · Cited by 18
Synaptotagmin 1 directs repetitive release by coupling vesicle exocytosis to the Rab3 cycle
Cheng, Y.-S., Wang, J.-M., Wang, Y., & Ding, M. (2015) · eLife · doi:10.7554/elife.05118 · Cited by 17
“The GTP-to-GDP conversion not only removes Rab3 from SVs, but also simultaneously dissociates Rab3 from its binding effectors, which disassembles the docking complex so that both Rab3 and Rab3 effectors can be recycled for the next round of release (Wang et al., 1997, 2000).”
BackgroundSelf-citationKim, K.-T., LEE, J. S., Lee, B. W., Seok, H.-S., Jeon, H. S., Kim, J. H., & Chung, J. (2013) · Biomedical Reports · doi:10.3892/br.2013.101 · Cited by 15
“RIMs have been shown to interact with multiple synaptic proteins, such as UNC-13 homolog B ( C. elegans ) (UNC13B, Munc13) (8), ELKS/Rab6-interacting/CAST family member 1 (ERC1, ELKS) (9,10), RIM-binding proteins (RIM-BPs) (11), α -liprins and synaptotagmin 1 (12-14).”
Lipid–protein interactions in exocytotic release of hormones and neurotransmitters
Rituper, B., Davletov, B. A., & Zorec, R. (2010) · Clinical Lipidology · doi:10.2217/clp.10.61 · Cited by 12
Retinitis Pigmentosa and Allied Disorders
Weleber, R. G., & Gregory-Evans, K. (2006) · Elsevier eBooks · doi:10.1016/b978-0-323-02598-0.50023-9 · Cited by 30
Rab3 and synaptotagmin proteins in the regulation of vesicle fusion and neurotransmitter release.
Wang, X.-C., Yu, D., Wang, H., Lei, Z., Zhai, Y., Sun, M., Chen, S., & Yin, P. (2022) · Life Science · doi:10.1016/j.lfs.2022.120995 · Cited by 15
Sclip, A., Acuna, C., Luo, F., & Südhof, T. C. (2018) · The EMBO Journal · doi:10.15252/embj.201798637 · Cited by 18
“The SH3-domains of RBPs directly bind to proline-rich sequences in RIMs and in L-, and P/Q-and N-type voltage-gated Ca 2+ -channels (Wang et al , 2000; Hibino et al , 2002; Kaeser et al , 2011).”
InfluentialSelf-citationSugita, S. (2004) · Methods · doi:10.1016/j.ymeth.2004.01.005 · Cited by 15
Self-citationRIM-Binding Proteins Are Required for Normal Sound-Encoding at Afferent Inner Hair Cell Synapses
Krinner, S., Predoehl, F., Burfeind, D., Vogl, C., & Moser, T. (2021) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2021.651935 · Cited by 31
“Specifically, the RIM-BPs’ two C-terminal SH3 domains interact with proline-rich motifs in the C-terminus of the CaVα1D subunit and RIMs (Wang et al., 2000; Hibino et al., 2002; Kaeser et al., 2011; Ortner et al., 2020; Petzoldt et al., 2020), while the N-terminal SH3 domain interacts with the proline-rich motif of ba…”
BackgroundInfluentialPresynaptic-like mechanisms and the control of insulin secretion in pancreatic β-cells.
Deng, K., & Thorn, P. (2022) · Cell Calcium · doi:10.1016/j.ceca.2022.102585 · Cited by 13
miRNA299 involvement in CYP11B2 expression in aldosterone-producing adenoma.
Nakano, Y., Yoshimoto, T., Watanabe, R., Murakami, M., Fukuda, T., Saito, K., Fujii, Y., Akashi, T., Tanaka, T., Yamada, T., et al. (2019) · European Journal of Endocrinology · doi:10.1530/eje-18-0882 · Cited by 10
Morrison, L. M., Edwards, S. L., Manning, L., Stec, N., Richmond, J. E., & Miller, K. G. (2018) · Genetics · doi:10.1534/genetics.118.300847 · Cited by 8
RIM3γ is a postsynaptic protein in the rat central nervous system
Liang, F., Zhang, B., Tang, J., Guo, J., Li, W., Ling, E., Chu, H., Wu, Y., Chan, Y. G., & Cao, Q. (2007) · The Journal of Comparative Neurology · doi:10.1002/cne.21403 · Cited by 9
“6 in Wang et al., 2000) most likely represented the distribution of the 42-kDa protein band, which has since proved to be an artifact of the immunoblotting experiments.”
BackgroundResultInfluentialSimilarity and Diversity of Presynaptic Molecules at Neuromuscular Junctions and Central Synapses
Takikawa, K., & Nishimune, H. (2022) · Biomolecules · doi:10.3390/biom12020179 · Cited by 16
“These results are consistent with the observation that RIMs bind to the synaptic vesicle protein Rab3s [31], the active zone protein Munc13s [40,48–50], Liprin-α [51], and RIM-binding proteins [52,53].”
ResultPiekut, T., Wong, Y. Y., Walker, S. E., Smith, C. L., Gauberg, J., Harracksingh, A. N., Lowden, C., Novogradac, B. B., Cheng, H. M., Spencer, G. E., et al. (2020) · Genome Biology and Evolution · doi:10.1093/gbe/evaa097 · Cited by 10
Uncoupling of Cav1.2 From Ca2+-Induced Ca2+Release and SK Channel Regulation in Pancreatic β-Cells
Wang, Y., Jarrard, R. E., Pratt, E. P. S., Guerra, M. L., Salyer, A. E., Lange, A. M., Soderling, I. M., & Hockerman, G. H. (2014) · Molecular Endocrinology · doi:10.1210/me.2013-1094 · Cited by 8
Self-citationOligomerization of rab/effector complexes in the regulation of vesicle trafficking.
Khan, A. R. (2013) · Progress in Molecular Biology and Translational Science · doi:10.1016/b978-0-12-386931-9.00021-0 · Cited by 9
Physical and functional interaction of noc2/rab3 in exocytosis.
Shibasaki, T., & Seino, S. (2005) · Methods in Enzymology · doi:10.1016/s0076-6879(05)03036-3 · Cited by 8
TSPO: an emerging role in appetite for a therapeutically promising biomarker
Wang, J., & Beecher, K. (2021) · Open Biology · doi:10.1098/rsob.210173 · Cited by 10
“Firstly, RIM-BP1 is highly expressed in brain regions associated with the limbic system [122], a key circuit in feeding-related reward [135].”
BackgroundAssay and functional interactions of Rim2 with Rab3.
Fukuda, M. (2005) · Methods in Enzymology · doi:10.1016/s0076-6879(05)03040-5 · Cited by 7
Spinal cord injury regulates circular RNA expression in axons
Siddiq, M. M., Toro, C. A., Johnson, N. P., Hansen, J., Xiong, Y., Mellado, W., Tolentino, R. E., Johnson, K., Jayaraman, G., Suhail, Z., et al. (2023) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2023.1183315 · Cited by 6
“For instance, the linear mRNA for Rims2 encodes a presynaptic protein that is important for neurotransmitter release, but the function of circRims2 is still unknown (18,19).”
BackgroundA Window into Domain Amplification Through Piccolo in Teleost Fish
Nonet, M. L. (2012) · G3 Genes Genomes Genetics · doi:10.1534/g3.112.003624 · Cited by 8
“Although Bassoon and Piccolo are unique in their large size, similar zinc finger, PDZ and C2 domains are also found in several other proteins localized to the presynaptic cytomatrix, including the proteins Rims1 and Rims2a (Wang et al. 1997, 2000; Jin and Garner 2008).”
Jackson, R. E., Compans, B., & Burrone, J. (2022) · Frontiers in Synaptic Neuroscience · doi:10.3389/fnsyn.2022.830583 · Cited by 5
Rimbp, a New Marker for the Nervous System of the Tunicate Ciona robusta
Coppola, U., Olivo, P., D’Aniello, E., Johnson, C. J., Stolfi, A., & Ristoratore, F. (2020) · Genes · doi:10.3390/genes11091006 · Cited by 4
“To date, Rimbp genes have been studied mainly in vertebrates [9,10,15] with expression in the brain reported both in newborn and adult rats [15].”
BackgroundUNC-10/SYD-2 links kinesin-3 to RAB-3-containing vesicles in the absence of the motor’s PH domainPreprint
Bayansan, O., Bhan, P., Chang, C.-Y., Barmaver, S. N., Shen, C.-P., & Wagner, O. I. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/723247 · Cited by 1
“The RIMS1 homolog in C. elegans is UNC-10 (Koushika et al., 2001) composed of an N-terminal zinc finger motif, a central PDZ domain, two C-terminal C2 domains (C2A and C2B) and a proline-rich SH3 motif (Wang et al., 2000).”
Sun, L., Bittner, M. A., & Holz, R. (2002) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2002.tb04468.x · Cited by 4
Dieck, S., Schmitz, F., & Brandstätter, J. (2007) · Molecular biology intelligence unit · doi:10.1007/978-0-387-39973-7_11 · Cited by 4
Miyano, R., Sakamoto, H., Hirose, K., & Sakaba, T. (2023) · eLife · doi:10.7554/elife.90799.3 · Cited by 3
“Rab3-interacting molecule-binding proteins (RIM-BPs) represent one principal, conserved family of AZ proteins and bind to RIMs and Ca 2+ channels ( Wang et al., 2000 ; Hibino et al., 2002 ).”
BackgroundMunc13-1, an active zone protein, regulates exocytosis in mast cells
Miura, K., Nomura, H., Nakanishi, M., & Hirashima, N. (2008) · Bioimages · doi:10.11169/bioimages.16.11 · Cited by 3
Reciprocal Regulation of Neuronal Calcium Channels by Synaptic Proteins
Weiss, N., & Zamponi, G. W. (2013) · Springer eBooks · doi:10.1007/978-94-007-6334-0_3 · Cited by 2
Presynaptic Mechanisms in Plasticity and Memory
Powell, C. M., & Castillo, P. E. (2008) · Elsevier eBooks · doi:10.1016/b978-012370509-9.00038-3 · Cited by 4
Sankaranarayanan, S., & Ryan, T. A. (2007) · Elsevier eBooks · doi:10.1016/b978-012369437-9/50010-4 · Cited by 2
Jánosi, B., Liewald, J., Yu, S.-C., Umbach, S., Alcantara, I. C., Bergs, A. C. F., Schneider, M., Shao, J., & Gottschalk, A. (2021) · bioRxiv · doi:10.1101/2021.02.01.429206 · Cited by 2
“5 affect the interaction of RIMB-1 and UNC-10/RIM, since it is mediated by the second SH3 141 domain (Wang et al., 2000), as well as the interaction with the UNC-2 VGCC, mediated by the 142 third SH3 domain.”
BackgroundSeney, M. L., Moon-Kim, S., Glausier, J., Hildebrand, M. A., Xue, X., Zong, W., Wang, J.-B., Shelton, M. A., Phan, B. N., Srinivasan, C., et al. (2020) · bioRxiv · doi:10.1101/2020.09.14.296707 · Cited by 2
“CADPS2 (39), RIMS3 (40)) (Data file S1), while the NAc was enriched for cytoskeletal remodeling and chemotaxis (e.”
MethodDer molekulare Mechanismus der Neurotransmitterfreisetzung und Nervenzell‐Synapsen (Nobel‐Aufsatz)
Südhof, T. C. (2014) · Angewandte Chemie · doi:10.1002/ange.201406359 · Cited by 3
Self-citationNakao, A., Hirano, M., Takada, Y., Kiyonaka, S., & Mori, Y. (2013) · Springer eBooks · doi:10.1007/978-94-007-6334-0_4 · Cited by 2
Regulation of dendritic spine morphogenesis and synapse formation by copines
Galic, M. (2006) · edoc (University of Basel) · doi:10.5451/unibas-004198769 · Cited by 1
La machinerie moléculaire de sécrétion des neurotransmetteurs
Südhof, T. C. (2015) · Biologie Aujourd hui · doi:10.1051/jbio/2015012 · Cited by 2
“Chez les mammifères, quatre gènes apparentées aux RIM sont exprimés, parmi lesquels deux seulement (les RIMs1 et RIMs2 ) produisent des protéines qui contiennent le domaine de liaison à Rab3 (Wang et al., 2000, 2002).”
InfluentialSelf-citationNetwork of Protein-Protein Interactions at the Presynaptic Active Zone
Ohtsuka, T. (2014) · Springer eBooks · doi:10.1007/978-4-431-55166-9_3 · Cited by 1
Synapse Formation in the Mammalian Central Nervous System
Yasuda, M., & Umemori, H. (2009) · Springer eBooks · doi:10.1007/978-0-387-92708-4_4 · Cited by 1
Molecular physiology of synaptic sound encoding at the first auditory synapse
Krinner, S. (2018) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-6793
“The two C-terminal SH3 domains interact with RIMs and the α1 subunits of voltage-gated P/Q-, N-, and L-type Cachannels (Hibino et al., 2002; Kaeser et al., 2011; Wang et al., 2000).”
BackgroundUNC-10 Regulates The Docking Step of DCV Exocytosis in C. elegans*
Wan-Juan, F. E. N. G., Zhou, W., Zhang, Y., Wu, Z., & Xu, T. (2012) · PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS · doi:10.3724/sp.j.1206.2011.00374
Dahlen, R. (2009) · doi:10.22028/d291-21084
“…für Rim2 von Dai et al. 2005 Coppola et al. 2001 vesikelassoziiert, Ca2+-Sensor, interagiert mit Syntaxin prolinreiche Sequenz zwischen 2 C-Domänen Rim-BPs Wang et al. 2000 C2B-Domäne alpha-Liprin Schoch et al. 2002 Gerüstprotein, bindet an Rim und LAR, Entwicklung von aktiver Zone?”
BackgroundPre- and Postsynaptic Assembly and Maturation
Sigrist, S. J., & Wichmann, C. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-397266-8.00008-9
Control of Neuronal Circuit Assembly by Gtpase Regulators
Sommer, J. E. (2011) · doi:10.7916/d81j9hz1
“In addition VGCCs bind to RIM (Rab3a interacting protein) and RBPs (RIM binding proteins) (Coppola et al., 2001; Hibino et al., 2002; Kiyonaka et al., 2007; Wang et al., 2000).”
BackgroundRab3A Interacting Molecules (RIMs)
Kaeser, P. S., & Powell, C. M. (2009) · Elsevier eBooks · doi:10.1016/b978-008045046-9.01353-x
Liprins, ELKS, and RIM-BP Proteins
Schoch, S., Mittelstaedt, T., & Zürner, M. (2009) · Elsevier eBooks · doi:10.1016/b978-008045046-9.01369-3
Analysis of the diversity of the postsynaptic membrane proteins neuroligins
Bolliger, M. (2001) · doi:10.3929/ethz-a-004238038
“, 2000), as well as shorter RIM isoforms containing only the C-terminal C2 domain (named NIM2 and NIM3) are also supposed to be involved in the regulation of neurotransmitter release (Wang et al., 2000).”
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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