Pub. Date : 2022 May 25
PMID : 35614056
8 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Here, we show that glucose availability regulates the central nutrient effector mTORC1 through intracellular leucine sensor leucyl-tRNA synthetase 1 (LARS1). | Leucine | leucyl-tRNA synthetase 1 | Homo sapiens |
| 2 | This modification inhibits the interaction of LARS1 with RagD GTPase and reduces the affinity of LARS1 for leucine by promoting phosphorylation of its leucine-binding site by the autophagy-activating kinase ULK1, decreasing mTORC1 activity. | Leucine | leucyl-tRNA synthetase 1 | Homo sapiens |
| 3 | This modification inhibits the interaction of LARS1 with RagD GTPase and reduces the affinity of LARS1 for leucine by promoting phosphorylation of its leucine-binding site by the autophagy-activating kinase ULK1, decreasing mTORC1 activity. | Leucine | leucyl-tRNA synthetase 1 | Homo sapiens |
| 4 | This modification inhibits the interaction of LARS1 with RagD GTPase and reduces the affinity of LARS1 for leucine by promoting phosphorylation of its leucine-binding site by the autophagy-activating kinase ULK1, decreasing mTORC1 activity. | Leucine | leucyl-tRNA synthetase 1 | Homo sapiens |
| 5 | The lack of LARS1 O-GlcNAcylation constitutively activates mTORC1, supporting its ability to sense leucine, and deregulates protein synthesis and leucine catabolism under glucose starvation. | Leucine | leucyl-tRNA synthetase 1 | Homo sapiens |
| 6 | The lack of LARS1 O-GlcNAcylation constitutively activates mTORC1, supporting its ability to sense leucine, and deregulates protein synthesis and leucine catabolism under glucose starvation. | Leucine | leucyl-tRNA synthetase 1 | Homo sapiens |
| 7 | This work demonstrates that LARS1 integrates leucine and glucose availability to regulate mTORC1 and the metabolic fate of leucine. | Leucine | leucyl-tRNA synthetase 1 | Homo sapiens |
| 8 | This work demonstrates that LARS1 integrates leucine and glucose availability to regulate mTORC1 and the metabolic fate of leucine. | Leucine | leucyl-tRNA synthetase 1 | Homo sapiens |