RIMS1

Regulating synaptic membrane exocytosis 1

PDB rendering based on 1zub.

Available structures
PDB	1zub, 2css

Identifiers

Symbols

RIMS1; CORD7; KIAA0340; MGC167823; MGC176677; RAB3IP2; RIM; RIM1

External IDs

OMIM: 606629 HomoloGene: 69176 GeneCards: RIMS1 Gene

Gene Ontology
Molecular function	• small GTPase regulator activity • protein binding • Rab GTPase binding • metal ion binding
Cellular component	• plasma membrane • plasma membrane • cell junction • presynaptic membrane • presynaptic membrane • synapse
Biological process	• protein complex assembly • intracellular protein transport • cellular membrane fusion • synaptic transmission • neurotransmitter secretion • visual perception • glutamate secretion • synaptic vesicle exocytosis • calcium ion-dependent exocytosis • regulated secretory pathway • secretion • response to stimulus
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

n/a

n/a

n/a

RefSeq (mRNA)

NM_001168407.1

n/a

RefSeq (protein)

NP_001161879.1

n/a

Location (UCSC)

Chr 6:
72.6 – 73.11 Mb

n/a

PubMed search

[1]

n/a

Regulating synaptic membrane exocytosis protein 1 is a protein that in humans is encoded by the RIMS1 gene.^[1]^[2]^[3]

RAB3A (MIM 179490), a member of the RAS gene superfamily, is a synaptic vesicle protein that regulates synaptic vesicle exocytosis. MUNC13 (UNC13; MIM 605836) and its isoforms are required for priming synaptic vesicles for exocytosis. The RIM family of active zone proteins likely function as protein scaffolds that help regulate vesicle exocytosis during short-term plasticity.[supplied by OMIM]^[3]

Interactions

RIMS1 has been shown to interact with UNC13B,^[4]^[5] RAB3A,^[4]^[6] ERC2^[5]^[7] and YWHAH.^[8]

References

^ Nagase T, Ishikawa K, Nakajima D, Ohira M, Seki N, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (Sep 1997). "Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro". DNA Res 4 (2): 141–50. doi:10.1093/dnares/4.2.141. PMID 9205841.
^ Coppola T, Magnin-Luthi S, Perret-Menoud V, Gattesco S, Schiavo G, Regazzi R (Aug 2001). "Direct interaction of the Rab3 effector RIM with Ca2+ channels, SNAP-25, and synaptotagmin". J Biol Chem 276 (35): 32756–62. doi:10.1074/jbc.M100929200. PMID 11438518.
^ ^a ^b "Entrez Gene: RIMS1 regulating synaptic membrane exocytosis 1". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=22999.
^ ^a ^b Betz, A; Thakur P, Junge H J, Ashery U, Rhee J S, Scheuss V, Rosenmund C, Rettig J, Brose N (Apr. 2001). "Functional interaction of the active zone proteins Munc13-1 and RIM1 in synaptic vesicle priming". Neuron (United States) 30 (1): 183–96. doi:10.1016/S0896-6273(01)00272-0. ISSN 0896-6273. PMID 11343654.
^ ^a ^b Ohtsuka, Toshihisa; Takao-Rikitsu Etsuko, Inoue Eiji, Inoue Marie, Takeuchi Masakazu, Matsubara Kaho, Deguchi-Tawarada Maki, Satoh Keiko, Morimoto Koji, Nakanishi Hiroyuki, Takai Yoshimi (Aug. 2002). "Cast: a novel protein of the cytomatrix at the active zone of synapses that forms a ternary complex with RIM1 and munc13-1". J. Cell Biol. (United States) 158 (3): 577–90. doi:10.1083/jcb.200202083. ISSN 0021-9525. PMC 2173811. PMID 12163476. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2173811.
^ Fukuda, Mitsunori (Apr. 2003). "Distinct Rab binding specificity of Rim1, Rim2, rabphilin, and Noc2. Identification of a critical determinant of Rab3A/Rab27A recognition by Rim2". J. Biol. Chem. (United States) 278 (17): 15373–80. doi:10.1074/jbc.M212341200. ISSN 0021-9258. PMID 12578829.
^ Takao-Rikitsu, Etsuko; Mochida Sumiko, Inoue Eiji, Deguchi-Tawarada Maki, Inoue Marie, Ohtsuka Toshihisa, Takai Yoshimi (Jan. 2004). "Physical and functional interaction of the active zone proteins, CAST, RIM1, and Bassoon, in neurotransmitter release". J. Cell Biol. (United States) 164 (2): 301–11. doi:10.1083/jcb.200307101. ISSN 0021-9525. PMC 2172332. PMID 14734538. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2172332.
^ Sun, Lei; Bittner Mary A, Holz Ronald W (Oct. 2003). "Rim, a component of the presynaptic active zone and modulator of exocytosis, binds 14-3-3 through its N terminus". J. Biol. Chem. (United States) 278 (40): 38301–9. doi:10.1074/jbc.M212801200. ISSN 0021-9258. PMID 12871946.

Kelsell RE, Gregory-Evans K, Gregory-Evans CY et al. (1998). "Localization of a gene (CORD7) for a dominant cone-rod dystrophy to chromosome 6q". Am. J. Hum. Genet. 63 (1): 274–9. doi:10.1086/301905. PMC 1377229. PMID 9634506. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1377229.
Betz A, Thakur P, Junge HJ et al. (2001). "Functional interaction of the active zone proteins Munc13-1 and RIM1 in synaptic vesicle priming". Neuron 30 (1): 183–96. doi:10.1016/S0896-6273(01)00272-0. PMID 11343654.
Liu X, Schrager JA, Lange GD, Marsh JW (2001). "HIV Nef-mediated cellular phenotypes are differentially expressed as a function of intracellular Nef concentrations". J. Biol. Chem. 276 (35): 32763–70. doi:10.1074/jbc.M101025200. PMID 11438519.
Daiho T, Yamasaki K, Saino T et al. (2001). "Mutations of either or both Cys876 and Cys888 residues of sarcoplasmic reticulum Ca2+-ATPase result in a complete loss of Ca2+ transport activity without a loss of Ca2+-dependent ATPase activity. Role of the CYS876-CYS888 disulfide bond". J. Biol. Chem. 276 (35): 32771–8. doi:10.1074/jbc.M101229200. PMID 11438520.
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Schoch S, Castillo PE, Jo T et al. (2002). "RIM1alpha forms a protein scaffold for regulating neurotransmitter release at the active zone". Nature 415 (6869): 321–6. doi:10.1038/415321a. PMID 11797009.
Ohtsuka T, Takao-Rikitsu E, Inoue E et al. (2002). "Cast: a novel protein of the cytomatrix at the active zone of synapses that forms a ternary complex with RIM1 and munc13-1". J. Cell Biol. 158 (3): 577–90. doi:10.1083/jcb.200202083. PMC 2173811. PMID 12163476. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2173811.
Wang Y, Liu X, Biederer T, Südhof TC (2002). "A family of RIM-binding proteins regulated by alternative splicing: Implications for the genesis of synaptic active zones". Proc. Natl. Acad. Sci. U.S.A. 99 (22): 14464–9. doi:10.1073/pnas.182532999. PMC 137906. PMID 12391317. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=137906.
Strausberg RL, Feingold EA, Grouse LH et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
Fukuda M (2003). "Distinct Rab binding specificity of Rim1, Rim2, rabphilin, and Noc2. Identification of a critical determinant of Rab3A/Rab27A recognition by Rim2". J. Biol. Chem. 278 (17): 15373–80. doi:10.1074/jbc.M212341200. PMID 12578829.
Wang Y, Südhof TC (2003). "Genomic definition of RIM proteins: evolutionary amplification of a family of synaptic regulatory proteins( small star, filled )". Genomics 81 (2): 126–37. doi:10.1016/S0888-7543(02)00024-1. PMID 12620390.
Johnson S, Halford S, Morris AG et al. (2003). "Genomic organisation and alternative splicing of human RIM1, a gene implicated in autosomal dominant cone-rod dystrophy (CORD7)". Genomics 81 (3): 304–14. doi:10.1016/S0888-7543(03)00010-7. PMID 12659814.
Sun L, Bittner MA, Holz RW (2003). "Rim, a component of the presynaptic active zone and modulator of exocytosis, binds 14-3-3 through its N terminus". J. Biol. Chem. 278 (40): 38301–9. doi:10.1074/jbc.M212801200. PMID 12871946.
Takao-Rikitsu E, Mochida S, Inoue E et al. (2004). "Physical and functional interaction of the active zone proteins, CAST, RIM1, and Bassoon, in neurotransmitter release". J. Cell Biol. 164 (2): 301–11. doi:10.1083/jcb.200307101. PMC 2172332. PMID 14734538. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2172332.
Beausoleil SA, Jedrychowski M, Schwartz D et al. (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=514446.
Barragan I, Marcos I, Borrego S, Antiñolo G (2005). "Molecular analysis of RIM1 in autosomal recessive Retinitis pigmentosa". Ophthalmic Res. 37 (2): 89–93. doi:10.1159/000084250. PMID 15746564.
Sisodiya SM, Thompson PJ, Need A et al. (2007). "Genetic enhancement of cognition in a kindred with cone–rod dystrophy due to RIMS1 mutation". J. Med. Genet. 44 (6): 373–80. doi:10.1136/jmg.2006.047407. PMC 2740882. PMID 17237123. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2740882.

PDB gallery

1zub: Solution Structure of the RIM1alpha PDZ Domain in Complex with an ELKS1b C-terminal Peptide

2css: Solution structure of the PDZ domain of human KIAA0340 protein

RIMS1

Interactions

References

Further reading