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Leucyl-tRNA synthetase (LRS) is a leucine sensor of the mTORC1 pathway.
The results showed a decrease in autophagy on addition of leucine, demonstrating crosstalk between leucine sensing, LRS translocation, RagD (show RRAGD Proteins) interaction, and mTORC1 activation.
the KMSKS catalytic loop affects the aminoacylation and editing capacities of leucyl-tRNA synthetase (show LARS2 Proteins)
Lack of a CP1 (show PCBP1 Proteins) hairpin in LeuRS (show LARS2 Proteins) led to complete loss of aminoacylation, amino acid activation, and tRNA binding; however, the mutants retained post-transfer editing.
the carboxy-terminal domain of human mitochondrial (mt) leucyl-tRNA synthetase (show LARS2 Proteins) can be used to correct mt dysfunctions caused by mt-tRNA mutations.
Identification of a mutation in LARS as a novel cause of infantile hepatopathy
This work demonstrates that LRS is a key mediator for amino acid signaling to mTORC1.
leucyl-tRNA synthetase (show LARS2 Proteins) requires its C-terminal domain for its interaction with arginyl-tRNA synthetase (show RARS Proteins) in the multi-tRNA synthetase complex
Results show that K600 in human leucyl-tRNA synthetase (show LARS2 Proteins) affects amino acid specificity and tRNA aminoacylation.
findings suggest that LARS1 may play roles in migration and growth of lung cancer cells, which suggest its potential implication in lung tumorigenesis
loss of LAR (show PTPRF Proteins) activity resulted in reduced activity of CDK1 (show CDK1 Proteins).
Study has identified LAR (show PTPRF Proteins) as a regulator of key signaling pathways, including mTOR (show FRAP1 Proteins) and JNK (show MAPK8 Proteins), and has significantly expanded the number of proteins regulated downstream of LAR (show PTPRF Proteins) phosphatase activity.
Chondroitin Sulfate Proteoglycans Negatively Modulate Spinal Cord Neural Precursor Cells by Signaling Through LAR (show PTPRF Proteins) and RPTPsigma (show PTPRS Proteins) and Modulation of the Rho/ROCK Pathway.
This study demonstrates the crucial role of LAR (show PTPRF Proteins) in restricting regrowth of injured CNS axons
Ptprs (show PTPRS Proteins) and Ptprf (show PTPRF Proteins) deficiency affects mandibular cell proliferation.
Inhibition of LAR (show PTPRF Proteins) attenuates palmitate-induced insulin (show INS Proteins) resistance in myotubes.
Deletion of LAR (show PTPRF Proteins) in knock-out mice or blockade of LAR (show PTPRF Proteins) with sequence-selective peptides significantly overcomes neurite growth restrictions of chondroitin sulfate proteoglycan (show Vcan Proteins) in neuronal cultures.
the crystal structures of the first and second immunoglobulin-like domains of the Drosophila type IIa receptor Dlar and its mouse homolog LAR (show PTPRF Proteins) were reported.
LAR reduces the basal c-Abl activity thereby allowing for platelet derived growth factor beta receptor kinase activation
LAR deficiency affected the differentiation & expansion of immature thymocytes, positive & negative selection, & a lower Ca2+ response. LAR is an important modulator of TCR signaling that controls thymocyte differentiation.
This gene encodes a cytosolic leucine-tRNA synthetase, a member of the class I aminoacyl-tRNA synthetase family. The encoded enzyme catalyzes the ATP-dependent ligation of L-leucine to tRNA(Leu). It is found in the cytoplasm as part of a multisynthetase complex and interacts with the arginine tRNA synthetase through its C-terminal domain. Alternatively spliced transcript variants of this gene have been found\; however, their full-length nature is not known.
, leucyl-tRNA synthetase
, leucine-tRNA ligase, mitochondrial
, leucyl-tRNA synthetase, mitochondrial
, cytoplasmic leucyl-tRNA synthetase
, cytosolic leucyl-tRNA synthetase
, leucine tRNA ligase 1, cytoplasmic
, leucine translase
, leucine--tRNA ligase, cytoplasmic
, leucine-tRNA ligase
, leucyl-tRNA synthetase, cytoplasmic
, proliferation-inducing gene 44
, leukocyte antigen-related (LAR) PTP receptor
, leukocyte common antigen related
, receptor-type tyrosine-protein phosphatase F