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

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

Se ha demostrado que RIMS1 interactúa con:

ERC2,[5]
RAB3A,[6]
UNC13A,[7]
UNC13B,[8][9] y
YHHAH[10]

Referencias

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.
«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

«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

Este artículo ha sido escrito por Wikipedia. El texto está disponible bajo la licencia Creative Commons - Atribución - CompartirIgual. Pueden aplicarse cláusulas adicionales a los archivos multimedia.

[1] 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.

[pmid9205841-2] «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.

[pmid11438518-3] «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.

[entrez-4] «Entrez Gene: RIMS1 regulating synaptic membrane exocytosis 1».

[pmid14734538-5] «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.

[pmid12578829-6] «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.

[7] «Protein unc-13 homolog A». UniProt.

[pmid12163476-8] «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.

[pmid11343654-9] «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.

[pmid12871946-10] «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.