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.
|Journal||Biochimica et Biophysica Acta - Molecular Cell Research|
|Publication status||Published - 2021 Jan|
Bibliographical noteFunding Information:
This work was supported by the Basic Science Research Program through the National Research Foundation (NRF) of Korea funded by the Ministry of Education [ 2018R1A6A1A03023718 ] and the NRF grant funded by the Korea government ( MSIT ) [ 2020R1A2C209958611 ] and by the Bio & Medical Technology Development Program of the NRF funded by the Ministry of Science & ICT [ 2020M3E5E2040282 ].
© 2020 Elsevier B.V.
All Science Journal Classification (ASJC) codes
- Molecular Biology
- Cell Biology