| Identification of LARS as an essential gene for osteosarcoma proliferation through large-Scale CRISPR-Cas9 screening database and experimental verification. | Identification of LARS as an essential gene for osteosarcoma proliferation through large-Scale CRISPR-Cas9 screening database and experimental verification.
Chen W, Lin Y, Jiang M, Wang Q, Shu Q., Free PMC Article | 08/27/2022 |
| O-GlcNAc modification of leucyl-tRNA synthetase 1 integrates leucine and glucose availability to regulate mTORC1 and the metabolic fate of leucine. | O-GlcNAc modification of leucyl-tRNA synthetase 1 integrates leucine and glucose availability to regulate mTORC1 and the metabolic fate of leucine.
Kim K, Yoo HC, Kim BG, Kim S, Sung Y, Yoon I, Yu YC, Park SJ, Kim JH, Myung K, Hwang KY, Kim S, Han JM., Free PMC Article | 06/11/2022 |
| Infantile Liver Failure Syndrome 1 associated with a novel variant of the LARS1 gene: Clinical, genetic, and functional characterization. | Infantile Liver Failure Syndrome 1 associated with a novel variant of the LARS1 gene: Clinical, genetic, and functional characterization.
Tabolacci E, Molinario C, Marangi G, Nobile V, Arena V, Mendes MI, Smith DEC, Salomons GS, Tana M, Costa S, Vento G, Genuardi M. | 01/22/2022 |
| Leucyl-tRNA synthetase 1 is required for proliferation of TSC-null cells. | Leucyl-tRNA synthetase 1 is required for proliferation of TSC-null cells.
Bae JH, Kim JH. | 11/22/2021 |
| Severe course with lethal hepatocellular injury and skeletal muscular dysgenesis in a neonate with infantile liver failure syndrome type 1 caused by novel LARS1 mutations. | Severe course with lethal hepatocellular injury and skeletal muscular dysgenesis in a neonate with infantile liver failure syndrome type 1 caused by novel LARS1 mutations.
Hirata K, Okamoto N, Ichikawa C, Inoue S, Nozaki M, Banno K, Takenouchi T, Suzuki H, Kosaki K. | 07/24/2021 |
| Genotypic diversity and phenotypic spectrum of infantile liver failure syndrome type 1 due to variants in LARS1. | Genotypic diversity and phenotypic spectrum of infantile liver failure syndrome type 1 due to variants in LARS1.
Lenz D, Smith DEC, Crushell E, Husain RA, Salomons GS, Alhaddad B, Bernstein JA, Bianzano A, Biskup S, Brennenstuhl H, Caldari D, Dikow N, Haack TB, Hanson-Kahn A, Harting I, Horn D, Hughes J, Huijberts M, Isidor B, Kathemann S, Kopajtich R, Kotzaeridou U, Küry S, Lainka E, Laugwitz L, Lupski JR, Posey JE, Reynolds C, Rosenfeld JA, Schröter J, Vansenne F, Wagner M, Weiß C, Wolffenbuttel BHR, Wortmann SB, Kölker S, Hoffmann GF, Prokisch H, Mendes MI, Staufner C. | 06/26/2021 |
| Molecular basis of the multifaceted functions of human leucyl-tRNA synthetase in protein synthesis and beyond. | Molecular basis of the multifaceted functions of human leucyl-tRNA synthetase in protein synthesis and beyond.
Liu RJ, Long T, Li H, Zhao J, Li J, Wang M, Palencia A, Lin J, Cusack S, Wang ED., Free PMC Article | 09/12/2020 |
| this study provides evidence for a role of leucyl-tRNA synthetase 1 (LARS1) in glucose-dependent control of leucine usage. | Glucose-dependent control of leucine metabolism by leucyl-tRNA synthetase 1.
Yoon I, Nam M, Kim HK, Moon HS, Kim S, Jang J, Song JA, Jeong SJ, Kim SB, Cho S, Kim Y, Lee J, Yang WS, Yoo HC, Kim K, Kim MS, Yang A, Cho K, Park HS, Hwang GS, Hwang KY, Han JM, Kim JH, Kim S. | 05/23/2020 |
| Leucyl-tRNA synthetase (LRS) is a leucine sensor of the mTORC1 pathway. | Control of leucine-dependent mTORC1 pathway through chemical intervention of leucyl-tRNA synthetase and RagD interaction.
Kim JH, Lee C, Lee M, Wang H, Kim K, Park SJ, Yoon I, Jang J, Zhao H, Kim HK, Kwon NH, Jeong SJ, Yoo HC, Kim JH, Yang JS, Lee MY, Lee CW, Yun J, Oh SJ, Kang JS, Martinis SA, Hwang KY, Guo M, Han G, Han JM, Kim S., Free PMC Article | 01/27/2018 |
| The results showed a decrease in autophagy on addition of leucine, demonstrating crosstalk between leucine sensing, LRS translocation, RagD interaction, and mTORC1 activation. | Leucine-induced localization of Leucyl-tRNA synthetase in lysosome membrane.
Choi H, Son JB, Kang J, Kwon J, Kim JH, Jung M, Kim SK, Kim S, Mun JY. | 10/28/2017 |
| the KMSKS catalytic loop affects the aminoacylation and editing capacities of leucyl-tRNA synthetase | Modulation of Aminoacylation and Editing Properties of Leucyl-tRNA Synthetase by a Conserved Structural Module.
Yan W, Ye Q, Tan M, Chen X, Eriani G, Wang ED., Free PMC Article | 08/8/2015 |
| Lack of a CP1 hairpin in LeuRS led to complete loss of aminoacylation, amino acid activation, and tRNA binding; however, the mutants retained post-transfer editing. | A bridge between the aminoacylation and editing domains of leucyl-tRNA synthetase is crucial for its synthetic activity.
Huang Q, Zhou XL, Hu QH, Lei HY, Fang ZP, Yao P, Wang ED., Free PMC Article | 10/25/2014 |
| the carboxy-terminal domain of human mitochondrial (mt) leucyl-tRNA synthetase can be used to correct mt dysfunctions caused by mt-tRNA mutations. | The isolated carboxy-terminal domain of human mitochondrial leucyl-tRNA synthetase rescues the pathological phenotype of mitochondrial tRNA mutations in human cells.
Perli E, Giordano C, Pisano A, Montanari A, Campese AF, Reyes A, Ghezzi D, Nasca A, Tuppen HA, Orlandi M, Di Micco P, Poser E, Taylor RW, Colotti G, Francisci S, Morea V, Frontali L, Zeviani M, d'Amati G., Free PMC Article | 10/18/2014 |
| Identification of a mutation in LARS as a novel cause of infantile hepatopathy | Identification of a mutation in LARS as a novel cause of infantile hepatopathy.
Casey JP, McGettigan P, Lynam-Lennon N, McDermott M, Regan R, Conroy J, Bourke B, O'Sullivan J, Crushell E, Lynch S, Ennis S. | 10/20/2012 |
| This work demonstrates that LRS is a key mediator for amino acid signaling to mTORC1. | Leucyl-tRNA synthetase is an intracellular leucine sensor for the mTORC1-signaling pathway.
Han JM, Jeong SJ, Park MC, Kim G, Kwon NH, Kim HK, Ha SH, Ryu SH, Kim S. | 06/9/2012 |
| hcLeuRS can charge RNALeu with non-cognate amino acids and exclude the incorrect products by multiple editing pathways. | Modular pathways for editing non-cognate amino acids by human cytoplasmic leucyl-tRNA synthetase.
Chen X, Ma JJ, Tan M, Yao P, Hu QH, Eriani G, Wang ED., Free PMC Article | 02/26/2011 |
| the introduction of bulky residues into the amino acid binding pocket failed to block deacylation of tRNA, indicating that the architecture of the amino acid binding pocket is different compared to that of other characterized LeuRSs | A paradigm shift for the amino acid editing mechanism of human cytoplasmic leucyl-tRNA synthetase.
Pang YL, Martinis SA., Free PMC Article | 01/21/2010 |
| Study of crystal structures of the editing domain from 2 eukaryotic cytosolic LeuRS; shows a conserved structural core containing the active site for hydrolysis, with distinct bacterial, archeal, or eukaryotic peripheral insertions. | Crystal structures of the human and fungal cytosolic Leucyl-tRNA synthetase editing domains: A structural basis for the rational design of antifungal benzoxaboroles.
Seiradake E, Mao W, Hernandez V, Baker SJ, Plattner JJ, Alley MR, Cusack S. | 01/21/2010 |
| findings suggest that LARS1 may play roles in migration and growth of lung cancer cells, which suggest its potential implication in lung tumorigenesis | Implication of leucyl-tRNA synthetase 1 (LARS1) over-expression in growth and migration of lung cancer cells detected by siRNA targeted knock-down analysis.
Shin SH, Kim HS, Jung SH, Xu HD, Jeong YB, Chung YJ., Free PMC Article | 01/21/2010 |
| We identified a novel G3283A transition in the mitochondrial DNA tRNA(Leu (UUR)) gene in a patient with ptosis, ophthalmoparesis and hyporeflexia. | A novel mutation in the mitochondrial DNA tRNA Leu (UUR) gene associated with late-onset ocular myopathy.
Maeso E, Rueda A, Jiménez S, Del Hoyo P, Martín R, Cabello A, Mendoza LM, Arenas J, Campos Y. | 01/21/2010 |
| leucyl-tRNA synthetase requires its C-terminal domain for its interaction with arginyl-tRNA synthetase in the multi-tRNA synthetase complex | The C-terminal appended domain of human cytosolic leucyl-tRNA synthetase is indispensable in its interaction with arginyl-tRNA synthetase in the multi-tRNA synthetase complex.
Ling C, Yao YN, Zheng YG, Wei H, Wang L, Wu XF, Wang ED. | 01/21/2010 |
| Results show that K600 in human leucyl-tRNA synthetase affects amino acid specificity and tRNA aminoacylation. | A single residue in leucyl-tRNA synthetase affecting amino acid specificity and tRNA aminoacylation.
Lue SW, Kelley SO., Free PMC Article | 01/21/2010 |