Leucine-sensing mechanism of leucyl-tRNA synthetase 1 for mTORC1 activation
Sulhee Kim, Ina Yoon, Jonghyeon Son, Junga Park, Kibum Kim, Jiho Lee, Sam‐Yong Park, Beom Sik Kang, Jung Min Han, Kwang Yeon Hwang, Sung‐Hoon Kim
Abstract
in the catalytic domain change the hydrogen bond network, leading to conformational change in the C-terminal domain, correlating with RagD association. Leucine binding to LARS1 is increased in the presence of ATP, further augmenting leucine-dependent interaction of LARS1 and RagD. Thus, this work unveils the structural basis for leucine-dependent long-range communication between the catalytic and RagD-binding domains of LARS1 for mTORC1 activation.
Topics & Concepts
LeucineChemistryBiochemistrymTORC1Amino acidConformational changeBiologyStereochemistrySignal transductionPI3K/AKT/mTOR pathwayRNA and protein synthesis mechanismsRNA modifications and cancerRNA Research and Splicing