Glutamyl-prolyl-tRNA synthetase 1 (EPRS1 (also appears as EPRS, GluProRS, GPRS in some sources))

Glutamyl-prolyl-tRNA synthetase 1 (EPRS1) is a multifunctional, bifunctional enzyme that catalyzes the aminoacylation of glutamic acid and proline onto their respective tRNAs, a key step in protein synthesis. In higher eukaryotes, EPRS1 is an integral component of the multi-tRNA synthetase complex (MSC) and displays noncanonical functions beyond aminoacylation. Upon cytokine stimulation (notably IFN-γ), EPRS1 is phosphorylated and released from the MSC, assembling into the GAIT complex, where it binds to select mRNA 3' UTR elements and silences translation of specific inflammatory genes. EPRS1 also orchestrates anti-inflammatory AKT signaling by recruiting and compartmentalizing AKT in early endosomes, and it has a documented role in the regulation of extracellular matrix proteins implicated in fibrosis. As both a central enzyme for translation and a mediator of immune and inflammatory pathways, EPRS1 is emerging as an important therapeutic target, particularly in disorders of inflammation and tissue remodeling.

Other names

EPRSEPRS1GluProRSGPRSglutamyl-prolyl tRNA synthetase

Direct enzymatic inhibition (e.g., halofuginone inhibits prolyl-tRNA synthetase activity); Modulation of post-translational modifications (phosphorylation of EPRS1 alters its function, particularly in immune signaling)