Aminoacyl-tRNA synthetases (ARSs) are a family of evolutionarily conserved housekeeping enzymes used for protein synthesis that have pivotal roles in the ligation of tRNA with their cognate amino acids. Recent advances in the structural and functional studies of ARSs have revealed many previously unknown biological functions beyond the classical catalytic roles. Sensing the sufficiency of intracellular nutrients such as amino acids, ATP, and fatty acids is a crucial aspect for every living organism, and it is closely connected to the regulation of diverse cellular physiologies. Notably, among ARSs, leucyl-tRNA synthetase 1 (LARS1) has been identified to perform specifically as a leucine sensor upstream of the amino acid-sensing pathway and thus participates in the coordinated control of protein synthesis and autophagy for cell growth. In addition to LARS1, other types of ARSs are also likely involved in the sensing and signaling of their cognate amino acids inside cells. Collectively, this review focuses on the mechanisms of ARSs interacting within amino acid signaling and proposes the possible role of ARSs as general intracellular amino acid sensors.

氨酰基-tRNA合成酶（ARS）是用于蛋白质合成的进化保守的管家酶家族，在tRNA与它们的同源氨基酸的连接中起关键作用。ARS的结构和功能研究的最新进展表明，除了经典的催化作用外，还存在许多以前未知的生物学功能。感知细胞内营养物质（例如氨基酸，ATP和脂肪酸）的充足性对于每个活生物体都是至关重要的方面，并且与多种细胞生理学的调节紧密相关。值得注意的是，在ARS中，已确定亮氨酰tRNA合成酶1（LARS1）在氨基酸传感途径的上游专门充当亮氨酸传感器，因此参与了蛋白质合成和细胞自噬的自控调控。除LARS1外，其他类型的ARS也可能参与细胞内其同源氨基酸的感测和信号传导。总的来说，这篇综述着重于ARS在氨基酸信号内相互作用的机制，并提出了ARS作为一般细胞内氨基酸传感器的可能作用。