Biology:MAGOH
 Generic protein structure example |
Protein mago nashi homolog is a protein that in humans is encoded by the MAGOH gene.[1][2]
Drosophila that have mutations in their mago nashi (grandchildless) gene produce progeny with defects in germplasm assembly and germline development. This gene encodes the mammalian mago nashi homolog. In mammals, mRNA expression is not limited to the germ plasm, but is expressed ubiquitously in adult tissues and can be induced by serum stimulation of quiescent fibroblasts.[2]
Interactions
MAGOH has been shown to interact with RBM8A[3][4] and NXF1.[4] In Drosophila melanogaster, Mago Nashi and Tsunagi/Y14 (core components of the exon junction complex) form a complex with a novel zinc finger protein, Ranshi, that has a role in oocyte differentiation.[5]
References
- ↑ "The mammalian homologue of mago nashi encodes a serum-inducible protein". Genomics 47 (2): 319–22. April 1998. doi:10.1006/geno.1997.5126. PMID 9479507.
- ↑ 2.0 2.1 "Entrez Gene: MAGOH mago-nashi homolog, proliferation-associated (Drosophila)". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4116.
- ↑ Zhao, X F; Nowak N J; Shows T B; Aplan P D (January 2000). "MAGOH interacts with a novel RNA-binding protein". Genomics (UNITED STATES) 63 (1): 145–8. doi:10.1006/geno.1999.6064. ISSN 0888-7543. PMID 10662555.
- ↑ 4.0 4.1 Kataoka, N; Diem M D; Kim V N; Yong J; Dreyfuss G (November 2001). "Magoh, a human homolog of Drosophila mago nashi protein, is a component of the splicing-dependent exon-exon junction complex". EMBO J. (England) 20 (22): 6424–33. doi:10.1093/emboj/20.22.6424. ISSN 0261-4189. PMID 11707413.
- ↑ "Mago Nashi, Tsunagi/Y14, and Ranshi form a complex that influences oocyte differentiation in Drosophila melanogaster". Dev. Biol. 339 (2): 307–19. Mar 2010. doi:10.1016/j.ydbio.2009.12.035. PMID 20045686.
Further reading
- "mago nashi mediates the posterior follicle cell-to-oocyte signal to organize axis formation in Drosophila". Development 124 (16): 3197–207. 1997. PMID 9272960.
- "MAGOH interacts with a novel RNA-binding protein". Genomics 63 (1): 145–8. 2000. doi:10.1006/geno.1999.6064. PMID 10662555.
- "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells". Genome Res. 10 (10): 1546–60. 2001. doi:10.1101/gr.140200. PMID 11042152.
- "Importin 13: a novel mediator of nuclear import and export". EMBO J. 20 (14): 3685–94. 2001. doi:10.1093/emboj/20.14.3685. PMID 11447110.
- "Drosophila Y14 shuttles to the posterior of the oocyte and is required for oskar mRNA transport". Curr. Biol. 11 (21): 1666–74. 2002. doi:10.1016/S0960-9822(01)00508-5. PMID 11696323.
- "Magoh, a human homolog of Drosophila mago nashi protein, is a component of the splicing-dependent exon-exon junction complex". EMBO J. 20 (22): 6424–33. 2002. doi:10.1093/emboj/20.22.6424. PMID 11707413.
- "Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis". RNA 8 (4): 426–39. 2002. doi:10.1017/S1355838202021088. PMID 11991638.
- "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. 2003. doi:10.1073/pnas.242603899. PMID 12477932. Bibcode: 2002PNAS...9916899M.
- "A novel mode of RBD-protein recognition in the Y14-Mago complex". Nat. Struct. Biol. 10 (6): 433–9. 2003. doi:10.1038/nsb926. PMID 12730685.
- "Structure of the Y14-Magoh core of the exon junction complex". Curr. Biol. 13 (11): 933–41. 2004. doi:10.1016/S0960-9822(03)00328-2. PMID 12781131.
- "eIF4A3 is a novel component of the exon junction complex". RNA 10 (2): 200–9. 2004. doi:10.1261/rna.5230104. PMID 14730019.
- "An eIF4AIII-containing complex required for mRNA localization and nonsense-mediated mRNA decay". Nature 427 (6976): 753–7. 2004. doi:10.1038/nature02351. PMID 14973490. Bibcode: 2004Natur.427..753P.
- "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization". Curr. Biol. 14 (16): 1436–50. 2004. doi:10.1016/j.cub.2004.07.051. PMID 15324660.
- "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. 2004. doi:10.1101/gr.2596504. PMID 15489334.
- "The exon junction core complex is locked onto RNA by inhibition of eIF4AIII ATPase activity". Nat. Struct. Mol. Biol. 12 (10): 861–9. 2005. doi:10.1038/nsmb990. PMID 16170325.
- "Exon-junction complex components specify distinct routes of nonsense-mediated mRNA decay with differential cofactor requirements". Mol. Cell 20 (1): 65–75. 2005. doi:10.1016/j.molcel.2005.08.012. PMID 16209946.
- "The DNA sequence and biological annotation of human chromosome 1". Nature 441 (7091): 315–21. 2006. doi:10.1038/nature04727. PMID 16710414. Bibcode: 2006Natur.441..315G.
- "Structure of the exon junction core complex with a trapped DEAD-box ATPase bound to RNA". Science 313 (5795): 1968–72. 2006. doi:10.1126/science.1131981. PMID 16931718. Bibcode: 2006Sci...313.1968A.
- "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. 2007. doi:10.1038/msb4100134. PMID 17353931.
- "Regulation of mRNA export by the PI3 kinase/AKT signal transduction pathway.". Mol. Biol. Cell 24 (8): 1208–21. 2013. doi:10.1091/mbc.E12-06-0450. PMID 23427269.
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