RTN1

From Wikipedia, the free encyclopedia

Reticulon 1

Identifiers

RTN1; NSP

External IDs

OMIM: 600865 MGI: 1933947 HomoloGene: 49654 GeneCards: RTN1 Gene

Gene Ontology
Molecular function	• signal transducer activity • protein binding
Cellular component	• integral to endoplasmic reticulum membrane
Biological process	• signal transduction • neuron differentiation
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

ENSG00000139970

ENSMUSG00000021087

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 14:
60.06 – 60.34 Mb

Chr 12:
72.21 – 72.41 Mb

PubMed search

Reticulon-1 is a protein that in humans is encoded by the RTN1 gene.^[1]^[2]

This gene belongs to the family of reticulon-encoding genes. Reticulons are associated with the endoplasmic reticulum, and are involved in neuroendocrine secretion or in membrane trafficking in neuroendocrine cells. Alternatively spliced transcript variants encoding different isoforms have been identified. Multiple promoters rather than alternative splicing of internal exons seem to be involved in this diversity.^[2]

Interactions

RTN1 has been shown to interact with BCL2-like 1^[3] and UGCG.^[4]

References

↑ Kools PF, Roebroek AJ, Van de Velde HJ, Marynen P, Bullerdiek J, Van de Ven WJ (February 1994). "Regional mapping of the human NSP gene to chromosome region 14q21→q22 by fluorescence in situ hybridization analysis". Cytogenet Cell Genet 66 (1): 48–50. doi:10.1159/000133662. PMID 8275708.
↑ 2.0 2.1 "Entrez Gene: RTN1 reticulon 1".
↑ Tagami, S; Eguchi Y, Kinoshita M, Takeda M, Tsujimoto Y (November 2000). "A novel protein, RTN-XS, interacts with both Bcl-XL and Bcl-2 on endoplasmic reticulum and reduces their anti-apoptotic activity". Oncogene (England) 19 (50): 5736–46. doi:10.1038/sj.onc.1203948. ISSN 0950-9232. PMID 11126360. Cite uses deprecated parameters (help)
↑ Di Sano, Federica; Fazi Barbara, Citro Gennaro, Lovat Penny E, Cesareni Gianni, Piacentini Mauro (July 2003). "Glucosylceramide synthase and its functional interaction with RTN-1C regulate chemotherapeutic-induced apoptosis in neuroepithelioma cells". Cancer Res. (United States) 63 (14): 3860–5. ISSN 0008-5472. PMID 12873973. Cite uses deprecated parameters (help)

Further reading

Senden NH, van de Velde HJ, Broers JL et al. (1994). "Cluster-10 lung-cancer antibodies recognize NSPs, novel neuro-endocrine proteins associated with membranes of the endoplasmic reticulum". Int. J. Cancer Suppl. 8: 84–8. doi:10.1002/ijc.2910570718. PMID 7515034.
Roebroek AJ, van de Velde HJ, Van Bokhoven A et al. (1993). "Cloning and expression of alternative transcripts of a novel neuroendocrine-specific gene and identification of its 135-kDa translational product". J. Biol. Chem. 268 (18): 13439–47. PMID 7685762.
van de Velde HJ (1995). "NSP-encoded reticulons, neuroendocrine proteins of a novel gene family associated with membranes of the endoplasmic reticulum". J. Cell. Sci. 107 (9): 2403–16. PMID 7844160.
van de Velde HJ (1994). "NSP-encoded reticulons are neuroendocrine markers of a novel category in human lung cancer diagnosis". Cancer Res. 54 (17): 4769–76. PMID 8062278.
Roebroek AJ, Ayoubi TA, Van de Velde HJ et al. (1997). "Genomic organization of the human NSP gene, prototype of a novel gene family encoding reticulons". Genomics 32 (2): 191–9. doi:10.1006/geno.1996.0105. PMID 8833145.
Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
Senden NH, Timmer ED, Boers JE et al. (1996). "Neuroendocrine-specific protein C (NSP-C): subcellular localization and differential expression in relation to NSP-A". Eur. J. Cell Biol. 69 (3): 197–213. PMID 8900485.
Hens J, Nuydens R, Geerts H et al. (1998). "Neuronal differentiation is accompanied by NSP-C expression". Cell Tissue Res. 292 (2): 229–37. doi:10.1007/s004410051054. PMID 9560466.
Tagami S, Eguchi Y, Kinoshita M et al. (2001). "A novel protein, RTN-XS, interacts with both Bcl-XL and Bcl-2 on endoplasmic reticulum and reduces their anti-apoptotic activity". Oncogene 19 (50): 5736–46. doi:10.1038/sj.onc.1203948. PMID 11126360.
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.
Oertle T, Klinger M, Stuermer CA, Schwab ME (2003). "A reticular rhapsody: phylogenic evolution and nomenclature of the RTN/Nogo gene family". FASEB J. 17 (10): 1238–47. doi:10.1096/fj.02-1166hyp. PMID 12832288.
Di Sano F, Fazi B, Citro G et al. (2003). "Glucosylceramide synthase and its functional interaction with RTN-1C regulate chemotherapeutic-induced apoptosis in neuroepithelioma cells". Cancer Res. 63 (14): 3860–5. PMID 12873973.
Ota T, Suzuki Y, Nishikawa T et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Iwahashi J, Hamada N (2004). "Human reticulon 1-A and 1-B interact with a medium chain of the AP-2 adaptor complex". Cell. Mol. Biol. (Noisy-le-grand). 49 Online Pub: OL467–71. PMID 14995077.
Hu Y, Fang X, Dunham SM et al. (2004). "90-kDa ribosomal S6 kinase is a direct target for the nuclear fibroblast growth factor receptor 1 (FGFR1): role in FGFR1 signaling". J. Biol. Chem. 279 (28): 29325–35. doi:10.1074/jbc.M311144200. PMID 15117958.
He W, Lu Y, Qahwash I et al. (2004). "Reticulon family members modulate BACE1 activity and amyloid-beta peptide generation". Nat. Med. 10 (9): 959–65. doi:10.1038/nm1088. PMID 15286784.
Gerhard DS, Wagner L, Feingold EA et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Rual JF, Venkatesan K, Hao T et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
Mannan AU, Boehm J, Sauter SM et al. (2007). "Spastin, the most commonly mutated protein in hereditary spastic paraplegia interacts with Reticulon 1 an endoplasmic reticulum protein". Neurogenetics 7 (2): 93–103. doi:10.1007/s10048-006-0034-4. PMID 16602018.

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