Glucose-dependent control of leucine metabolism by leucyl-tRNA synthetase 1.
Animals
Autophagy-Related Protein-1 Homolog
/ genetics
Energy Metabolism
Fibroblasts
Glucose
/ metabolism
HEK293 Cells
HeLa Cells
Humans
Leucine
/ metabolism
Leucine-tRNA Ligase
/ metabolism
Lysosomes
/ metabolism
Mechanistic Target of Rapamycin Complex 1
/ metabolism
Mice
Monomeric GTP-Binding Proteins
/ metabolism
Phosphorylation
Signal Transduction
Journal
Science (New York, N.Y.)
ISSN: 1095-9203
Titre abrégé: Science
Pays: United States
ID NLM: 0404511
Informations de publication
Date de publication:
10 01 2020
10 01 2020
Historique:
received:
24
05
2018
revised:
20
03
2019
accepted:
14
11
2019
pubmed:
30
11
2019
medline:
19
5
2020
entrez:
30
11
2019
Statut:
ppublish
Résumé
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 (ULK1) 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 LARS1-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.
Identifiants
pubmed: 31780625
pii: science.aau2753
doi: 10.1126/science.aau2753
doi:
Substances chimiques
Autophagy-Related Protein-1 Homolog
EC 2.7.11.1
Mechanistic Target of Rapamycin Complex 1
EC 2.7.11.1
Monomeric GTP-Binding Proteins
EC 3.6.5.2
LARS protein, mouse
EC 6.1.1.4
LARS1 protein, human
EC 6.1.1.4
Leucine-tRNA Ligase
EC 6.1.1.4
Leucine
GMW67QNF9C
Glucose
IY9XDZ35W2
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
205-210Commentaires et corrections
Type : CommentIn
Type : CommentIn
Informations de copyright
Copyright © 2020 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works.