RBM8A (E5Z8T) Rabbit mAb #5386

The exon junction complex (EJC) plays a critical role in splicing, translation, mRNA localization, as well as nonsense-mediated decay. It comprises three core proteins, eIF4A3, Mago homolog (MAGOH), and RBM8A, as well as the peripheral factor MLN51 (1-4). The EJC proteins act as a binding platform for auxiliary factors that control mRNA export and nonsense-mediated decay (NMD) (5). RBM8A and MAGOH bind to key NMD factor UPF3B and dock around 20 nucleosides upstream of exon-exon junctions, which helps facilitate proper splicing and NMD functions (6-8). During translation, ribosomes will determine whether NMD factors are needed when encountering a stop codon. If EJCs exist downstream of the stop codon, the ribosome will recruit the SURF complex, and UPF1 phosphorylation will help facilitate the decay of prematurely terminated mRNAs (9,10). The EJC also is involved in the cell cycle as eIF4A3 is phosphorylated at threonine 163 by CDK1 and CDK2, which inhibits NMD function and prevents complex formation (11,12). Aberrant RBM8A expression causes cell cycle dysfunction, while low MAGOH expression affects neurological development and proliferation (13,14). EJC members have been implicated in a wide array of diseases and cancer, including hepatocellular carcinoma, glioblastoma, and neurological disorders (15-17).