Glucose-dependent control of leucine metabolism by leucyl-tRNA synthetase 1

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Despite the importance of glucose and amino acids for energy metabolism, interactions between the two nutrients are not well understood. We provide evidence for a role of leucyl-tRNA synthetase 1 (LARS1) in glucose-dependent control of leucine usage. Upon glucose starvation, LARS1 was phosphorylated by Unc-51 like autophagy activating kinase 1 (ULKI) at the residues crucial for leucine binding. The phosphorylated LARS1 showed decreased leucine binding, which may inhibit protein synthesis and help save energy. Leucine that is not used for anabolic processes may be available for catabolic pathway energy generation. The LARSi-mediated changes in leucine utilization might help support cell survival under glucose deprivation. Thus, depending on glucose availability, LARS1 may help regulate whether leucine is used for protein synthesis or energy production.
Publisher
AMER ASSOC ADVANCEMENT SCIENCE
Issue Date
2020-01
Language
English
Article Type
Article
Citation

SCIENCE, v.367, no.6474, pp.205

ISSN
0036-8075
DOI
10.1126/science.aau2753
URI
http://hdl.handle.net/10203/272089
Appears in Collection
CH-Journal Papers(저널논문)
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