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Query: EC:6.1.1.4 (
leucyl-tRNA synthetase
)
297
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Amino acids are required for activation of the mammalian target of rapamycin (mTOR) kinase, which regulates protein translation, cell size, and autophagy. However, the amino acid sensor that directly couples intracellular amino acid-mediated signaling to mTORC1 is unknown. Here we show that
leucyl-tRNA synthetase
(
LRS
) plays a critical role in amino acid-induced mTORC1 activation by sensing intracellular leucine concentration and initiating molecular events leading to mTORC1 activation. Mutation of
LRS
amino acid residues important for leucine binding renders the mTORC1 pathway insensitive to intracellular levels of amino acids. We show that
LRS
directly binds to Rag GTPase, the mediator of amino acid signaling to mTORC1, in an amino acid-dependent manner and functions as a
GTPase-activating protein
(
GAP
) for Rag GTPase to activate mTORC1. This work demonstrates that
LRS
is a key mediator for amino acid signaling to mTORC1.
...
PMID:Leucyl-tRNA synthetase is an intracellular leucine sensor for the mTORC1-signaling pathway. 2250 Jul 35
