Arginyl-tRNA--protein transferase 1 (ATE1)

Arginyl-tRNA--protein transferase 1 (ATE1) is a highly conserved enzyme responsible for the posttranslational modification of proteins by transferring an arginine residue from arginyl-tRNA to specific target proteins, mostly to N-terminal acidic residues such as aspartate or glutamate, as well as oxidized cysteine, and less frequently to internal side chains[1][3][5]. This modification, termed arginylation, serves as a critical signal (N-degron) for protein recognition in major degradation pathways including the ubiquitin-proteasome and autophagy-lysosome systems, influencing protein stability, turnover, and cellular response to stress[1][3]. ATE1 is essential for normal cardiovascular and developmental processes, with knockout models showing embryonic lethality, heart defects, and neurological changes[3][4]. It also impacts cytoskeleton dynamics, cell motility, and neuroprotection. ATE1 forms distinct molecular complexes in vivo, is ATP-independent in its activity, and controls the half-life of diverse protein substrates by linking protein synthesis, cellular metabolism, and protein degradation[1][2][3][4][5]. Currently, no drugs are known to directly target ATE1, and there are no established biomarkers or approved therapeutics. Dysregulation can have severe consequences in development and tissue function.

Other names

Arginyltransferase 1R-transferase 1Arginine-tRNA--protein transferase 1arginyl-tRNA--protein transferase 1arginyl-tRNA-protein transferaseATE1

Covalent transfer of arginine from arginyl-tRNA to protein substrates, primarily at the N-terminal aspartate, glutamate, or oxidized cysteine residues (N-terminal arginylation) and occasionally internal acidic residues. This generates N-degrons that regulate further protein fate through degradation pathways[1][3][5].