High impact information on MAGOH

• In contrast, REF/Aly, Y14, and Magoh remain stably bound to spliced mRNA, indicating that these three proteins are components of the EJC core [1].
• Most interesting, we have identified a region within MLN51 sufficient to bind RNA, to interact with Magoh and spliced mRNA, and to address the protein to nuclear speckles [2].
• Of note, MAGOH mRNA expression is not limited to germ plasm, but is expressed ubiquitously in adult tissues and can be induced by serum stimulation of quiescent fibroblasts [3].
• MAGOH was mapped to chromosome 1p33-p34 in the human and a syntenic region of chromosome 4 in the mouse [3].
• The predicted amino acid sequence of mouse and human MAGOH are completely identical; MAGOH homologues from the nematode Caenorhabditis elegans and rice grain Oryza sativa also show a remarkable degree of amino acid conservation [3].

Physical interactions of MAGOH

• Magoh binds avidly and directly to Y14 and TAP, but not to other known components of the complex, and is found in Y14-containing mRNPs in vivo [4].

Other interactions of MAGOH

• The stable association of the recombinant EJC core with RNA is maintained by inhibition of eIF4AIII ATPase activity by MAGOH-Y14 [5].

Analytical, diagnostic and therapeutic context of MAGOH

• In contrast, Y14 and magoh, which remain stably associated with mRNA after export to the cytoplasm, join the EJC during or after completion of exon-exon ligation [6].

References