RIMS1

Jump to navigation Jump to search
The printable version is no longer supported and may have rendering errors. Please update your browser bookmarks and please use the default browser print function instead.


Regulating synaptic membrane exocytosis 1
File:PBB Protein RIMS1 image.jpg
PDB rendering based on 1zub.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols RIMS1 ; RIM; CORD7; KIAA0340; RAB3IP2; RIM1
External IDs Template:OMIM5 HomoloGene69176
RNA expression pattern
File:PBB GE RIMS1 216184 s at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Regulating synaptic membrane exocytosis 1, also known as RIMS1, is a human gene.[1]

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][1]

References

  1. 1.0 1.1 "Entrez Gene: RIMS1 regulating synaptic membrane exocytosis 1".

Further reading

  • Nagase T, Ishikawa K, Nakajima D; et al. (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. PMID 9205841.
  • 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. PMID 9634506.
  • 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. PMID 11343654.
  • Coppola T, Magnin-Luthi S, Perret-Menoud V; et al. (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.
  • 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.
  • Tsuji M, Inanami O, Kuwabara M (2001). "Induction of neurite outgrowth in PC12 cells by alpha -phenyl-N-tert-butylnitron through activation of protein kinase C and the Ras-extracellular signal-regulated kinase pathway". J. Biol. Chem. 276 (35): 32779–85. doi:10.1074/jbc.M101403200. PMID 11438521.
  • Dierks H, Kolanus J, Kolanus W (2001). "Actin cytoskeletal association of cytohesin-1 is regulated by specific phosphorylation of its carboxyl-terminal polybasic domain". J. Biol. Chem. 276 (40): 37472–81. doi:10.1074/jbc.M101502200. PMID 11438522.
  • 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. PMID 12163476.
  • 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. PMID 12391317.
  • 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. PMID 12477932.
  • 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. 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. 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. PMID 14734538.
  • 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. PMID 15302935.
  • 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. PMID 17237123.

Template:WikiDoc Sources