RIMS1
La proteína de regulación de la exocitosis-1 de la membrana sináptica[1] (RIMS1) es una proteína que en los humanos está codificada por el gen RIMS1.[2][3][4]
Función[editar]
RAB3A (MIM 179490), miembro de la superfamilia de genes Ras, es una proteína de vesícula sináptica que regula la exocitosis de vesícula sináptica. MUNC13 (UNC13; MIM 605836) y sus isoformas son necesarias para preparar vesículas sinápticas para la exocitosis. La familia RIM de proteínas de la zona activa probablemente funcione como andamios de proteínas que ayudan a regular la exocitosis vesicular durante la plasticidad a corto plazo.[Suministrado por OMIM][4]
Interacciones[editar]
Se ha demostrado que RIMS1 interactúa con:
Referencias[editar]
- ↑ Plaza Serón, María del Carmen (2016). Reacciones de hipersensibilidad por intolerancia cruzada a antiinflamatorios no esteroideos: relación fenotipo-genotipo. Universidad de Málaga. p. 29. Consultado el 12 de febrero de 2020.
- ↑ «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. September 1997. PMID 9205841. doi:10.1093/dnares/4.2.141.
- ↑ «Direct interaction of the Rab3 effector RIM with Ca2+ channels, SNAP-25, and synaptotagmin». J Biol Chem 276 (35): 32756-62. August 2001. PMID 11438518. doi:10.1074/jbc.M100929200.
- ↑ a b «Entrez Gene: RIMS1 regulating synaptic membrane exocytosis 1».
- ↑ «Physical and functional interaction of the active zone proteins, CAST, RIM1, and Bassoon, in neurotransmitter release». J. Cell Biol. 164 (2): 301-11. January 2004. PMC 2172332. PMID 14734538. doi:10.1083/jcb.200307101.
- ↑ «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. April 2003. PMID 12578829. doi:10.1074/jbc.M212341200.
- ↑ «Protein unc-13 homolog A». UniProt.
- ↑ «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. August 2002. PMC 2173811. PMID 12163476. doi:10.1083/jcb.200202083.
- ↑ «Functional interaction of the active zone proteins Munc13-1 and RIM1 in synaptic vesicle priming». Neuron 30 (1): 183-96. April 2001. PMID 11343654. doi:10.1016/s0896-6273(01)00272-0.
- ↑ «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. October 2003. PMID 12871946. doi:10.1074/jbc.M212801200.
Lectura adicional[editar]
- «Localization of a gene (CORD7) for a dominant cone-rod dystrophy to chromosome 6q». Am. J. Hum. Genet. 63 (1): 274-9. 1998. PMC 1377229. PMID 9634506. doi:10.1086/301905.
- «Functional interaction of the active zone proteins Munc13-1 and RIM1 in synaptic vesicle priming». Neuron 30 (1): 183-96. 2001. PMID 11343654. doi:10.1016/S0896-6273(01)00272-0.
- «HIV Nef-mediated cellular phenotypes are differentially expressed as a function of intracellular Nef concentrations». J. Biol. Chem. 276 (35): 32763-70. 2001. PMID 11438519. doi:10.1074/jbc.M101025200.
- «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. 2001. PMID 11438520. doi:10.1074/jbc.M101229200.
- «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. 2001. PMID 11438521. doi:10.1074/jbc.M101403200.
- «Actin cytoskeletal association of cytohesin-1 is regulated by specific phosphorylation of its carboxyl-terminal polybasic domain». J. Biol. Chem. 276 (40): 37472-81. 2001. PMID 11438522. doi:10.1074/jbc.M101502200.
- «RIM1alpha forms a protein scaffold for regulating neurotransmitter release at the active zone». Nature 415 (6869): 321-6. 2002. PMID 11797009. doi:10.1038/415321a.
- «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. 2002. PMC 2173811. PMID 12163476. doi:10.1083/jcb.200202083.
- «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. 2002. PMC 137906. PMID 12391317. doi:10.1073/pnas.182532999.
- «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. 2003. PMID 12578829. doi:10.1074/jbc.M212341200.
- «Genomic definition of RIM proteins: evolutionary amplification of a family of synaptic regulatory proteins( small star, filled )». Genomics 81 (2): 126-37. 2003. PMID 12620390. doi:10.1016/S0888-7543(02)00024-1.
- «Genomic organisation and alternative splicing of human RIM1, a gene implicated in autosomal dominant cone-rod dystrophy (CORD7)». Genomics 81 (3): 304-14. 2003. PMID 12659814. doi:10.1016/S0888-7543(03)00010-7.
- «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. 2003. PMID 12871946. doi:10.1074/jbc.M212801200.
- «Physical and functional interaction of the active zone proteins, CAST, RIM1, and Bassoon, in neurotransmitter release». J. Cell Biol. 164 (2): 301-11. 2004. PMC 2172332. PMID 14734538. doi:10.1083/jcb.200307101.
- «Large-scale characterization of HeLa cell nuclear phosphoproteins». Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130-5. 2004. PMC 514446. PMID 15302935. doi:10.1073/pnas.0404720101.
- «Molecular analysis of RIM1 in autosomal recessive Retinitis pigmentosa». Ophthalmic Res. 37 (2): 89-93. 2005. PMID 15746564. doi:10.1159/000084250.
- «Genetic enhancement of cognition in a kindred with cone–rod dystrophy due to RIMS1 mutation». J. Med. Genet. 44 (6): 373-80. 2007. PMC 2740882. PMID 17237123. doi:10.1136/jmg.2006.047407.
Datos: Q18036647