InterPro domain: IPR004023

This family was originally identified in Drosophila and called mago nashi, it is a strict maternal effect, grandchildless-like, gene [ 1 ]. The protein is an integral member of the exon junction complex (EJC). The EJC is a multiprotein complex that is deposited on spliced mRNAs after intron removal at a conserved position upstream of the exon-exon junction, and transported to the cytoplasm where it has been shown to influence translation, surveillance, and localization of the spliced mRNA. It consists of four core proteins (eIF4AIII, Barentsz [Btz], Mago, and Y14), mRNA, and ATP and is supposed to be a binding platform for more peripherally and transiently associated factors along mRNA travel. Mago and Y14 form a stable heterodimer that stabilizes the complex by inhibiting eIF4AIII's ATPase activity. Mago-Y14 heterodimer has been shown to interact with the cytoplasmic protein PYM, an EJC disassembly factor, and specifically binds to the karyopherin nuclear receptor importin 13 [ 2 , 3 , 4 , 5 , 6 , 7 , 8 , 9 , 9 , 10 , 11 , 12 , 13 , 14 , 15 , 16 , 17 ].

The human homologue has been shown to interact with an RNA binding protein, ribonucleoprotein rbm8 ( Q9Y5S9 ) [ 18 ]. An RNAi knockout of the Caenorhabditis elegans homologue causes masculinization of the germ line (Mog phenotype) hermaphrodites, suggesting it is involved in hermaphrodite germ-line sex determination [ 18 ] but the protein is also found in hermaphrodites and other organisms without a sexual differentiation.

1. Mutations in a newly identified Drosophila melanogaster gene, mago nashi, disrupt germ cell formation and result in the formation of mirror-image symmetrical double abdomen embryos. Development 113, 373-84
2. Structural insights into the exon junction complex. Curr. Opin. Struct. Biol. 18, 112-9
3. The exon junction complex differentially marks spliced junctions. Nat. Struct. Mol. Biol. 17, 1269-71
4. Exon junction complex subunits are required to splice Drosophila MAP kinase, a large heterochromatic gene. Cell 143, 238-50
5. A new function for nonsense-mediated mRNA-decay factors. Trends Genet. 21, 143-8
6. Structure of the Y14-Magoh core of the exon junction complex. Curr. Biol. 13, 933-41
7. The ever-increasing complexities of the exon junction complex. Curr. Opin. Cell Biol. 16, 279-84
8. EJCs at the heart of translational control. Cell 133, 213-6
9. mag-1, a homolog of Drosophila mago nashi, regulates hermaphrodite germ-line sex determination in Caenorhabditis elegans. Dev. Biol. 218, 172-82
10. MAGOH interacts with a novel RNA-binding protein. Genomics 63, 145-8
11. Magoh, a human homolog of Drosophila mago nashi protein, is a component of the splicing-dependent exon-exon junction complex. EMBO J. 20, 6424-33
12. mago nashi mediates the posterior follicle cell-to-oocyte signal to organize axis formation in Drosophila. Development 124, 3197-207
13. A novel mode of RBD-protein recognition in the Y14-Mago complex. Nat. Struct. Biol. 10, 433-9
14. Molecular insights into the interaction of PYM with the Mago-Y14 core of the exon junction complex. EMBO Rep. 5, 304-10
15. Identification and expression pattern of mago nashi during zebrafish development. Gene Expr. Patterns 5, 265-72
16. Molecular control of serial module formation along the apical-basal axis in the sponge Lubomirskia baicalensis: silicateins, mannose-binding lectin and mago nashi. Dev. Genes Evol. 216, 229-42
17. Molecular identification and characterization of Tcmago and TcY14 in Taiwania (Taiwania cryptomerioides). Tree Physiol. 27, 1261-71