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Mago-nashi homolog, proliferation-associated

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. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Y14, caspase-3, MLN51, eIF4AIII, SR protein
Papers on Magoh
Prolonged Mitosis of Neural Progenitors Alters Cell Fate in the Developing Brain.
Silver et al., Durham, United States. In Neuron, Feb 2016
Live imaging of progenitors from a neurogenesis mutant, Magoh(+/-), reveals that mitotic delay significantly correlates with preferential production of neurons instead of progenitors, as well as apoptotic progeny.
Phosphorylation status of human RNA-binding protein 8A in cells and its inhibitory regulation by Magoh.
Tomosugi et al., Kanazawa, Japan. In Exp Biol Med (maywood), Apr 2015
The RNA-binding protein 8A (RBM8A)-mago-nashi homolog, proliferation-associated (Magoh) complex is a component of the exon junction complex (EJC) required for mRNA metabolism involving nonsense-mediated mRNA decay (NMD).
A combined proteomics/genomics approach links hepatitis C virus infection with nonsense-mediated mRNA decay.
Ott et al., San Francisco, United States. In Mol Cell, Feb 2015
Expression of core prevents WIBG from binding its regular interaction partners Y14 and Magoh, two known mediators of the nonsense-mediated mRNA decay pathway.
A critical role of RBM8a in proliferation and differentiation of embryonic neural progenitors.
Mao et al., Nanning, China. In Neural Dev, 2014
This mechanism depends on several core factors in the exon junction complex (EJC), eIF4A3, RBM8a, Magoh, and BTZ, as well as peripheral factors to distinguish premature stop codons (PTCs) from normal stop codons in transcripts.
Overexpression of MLN51 triggers P-body disassembly and formation of a new type of RNA granules.
Gillet et al., Rennes, France. In J Cell Sci, 2014
Unlike the three other EJC core components [eIF4AIII, Magoh and Y14 (also known as RBM8A)], MLN51 is mainly located in the cytoplasm, where it plays a key role in the assembly of stress granules.
Generation of a Magoh conditional allele in mice.
Silver et al., Durham, United States. In Genesis, 2014
Magoh encodes a core component of the exon junction complex (EJC), which binds mRNA and regulates mRNA metabolism.
RNA-binding protein RBM8A (Y14) and MAGOH localize to centrosome in human A549 cells.
Tomosugi et al., Kanazawa, Japan. In Histochem Cell Biol, 2014
RBM8A (Y14) is carrying RNA-binding motif and forms the tight heterodimer with MAGOH.
Transcriptome-wide modulation of splicing by the exon junction complex.
Le Hir et al., In Genome Biol, 2013
The four core proteins, eIF4A3, Magoh, Y14 and MLN51, are stably bound to mRNAs during their lifecycle, serving as a binding platform for other nuclear and cytoplasmic proteins.
Depletion of RNA-binding protein RBM8A (Y14) causes cell cycle deficiency and apoptosis in human cells.
Tomosugi et al., Kanazawa, Japan. In Exp Biol Med (maywood), 2013
RBM8A (Y14) contains an RNA-binding motif and forms a tight heterodimer with Magoh.
Two mammalian MAGOH genes contribute to exon junction complex composition and nonsense-mediated decay.
Gehring et al., Köln, Germany. In Rna Biol, 2013
EJCs are deposited on messenger RNAs (mRNAs) during splicing and their core consists of eIF4A3, MLN51, Y14, and MAGOH.
Exon junction complex subunits are required to splice Drosophila MAP kinase, a large heterochromatic gene.
Treisman et al., United States. In Cell, 2010
MAPK is the primary functional target of mago in eye development; in cultured cells, Mago knockdown disproportionately affects other large genes located in heterochromatin
Mago Nashi, Tsunagi/Y14, and Ranshi form a complex that influences oocyte differentiation in Drosophila melanogaster.
Boswell et al., Austin, United States. In Dev Biol, 2010
Mago Nashi, Tsunagi/Y14, and Ranshi form a complex that influences oocyte differentiation in Drosophila melanogaster
Disassembly of exon junction complexes by PYM.
Hentze et al., Heidelberg, Germany. In Cell, 2009
This disassembly involves PYM binding to the EJC proteins MAGOH-Y14.
The exon-junction complex proteins, Y14 and MAGOH regulate STAT3 activation.
Matsuda et al., Sapporo, Japan. In Biochem Biophys Res Commun, 2009
These results indicate that MAGOH regulates the transcriptional activation of STAT3 by interfering complex formation between STAT3 and Y14.
Mago Nashi and Tsunagi/Y14, respectively, regulate Drosophila germline stem cell differentiation and oocyte specification.
Boswell et al., Boulder, United States. In Dev Biol, 2007
mago nashi is required for germline stem cell differentiation, but surprisingly mago nashi functions independently of tsunagi/Y14 in this process
Structure of the exon junction core complex with a trapped DEAD-box ATPase bound to RNA.
Andersen et al., Århus, Denmark. In Science, 2006
crystal structure of a tetrameric exon junction core complex containing the DEAD-box adenosine triphosphatase eukaryotic initiation factor 4AIII bound to an ATP analog, MAGOH, Y14, a fragment of MLN51, and a polyuracil mRNA mimic
A new function for nonsense-mediated mRNA-decay factors.
Wilkinson, Houston, United States. In Trends Genet, 2005
Surprisingly, recent evidence strongly suggests that the NMD factors UPF1, UPF2, UPF3B, RNPS1, Y14 and MAGOH also promote translation of normal mRNAs in mammalian cells.
Splicing of oskar RNA in the nucleus is coupled to its cytoplasmic localization.
Ephrussi et al., Heidelberg, Germany. In Nature, 2004
The nuclear shuttling proteins Y14/Tsunagi and Mago nashi are required for oskar mRNA localization, and they co-localize with oskar mRNA at the posterior pole of the oocyte.
An eIF4AIII-containing complex required for mRNA localization and nonsense-mediated mRNA decay.
Izaurralde et al., Cambridge, United Kingdom. In Nature, 2004
The mammalian Mago (also known as Magoh)-Y14 heterodimer is a component of the exon junction complex.
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