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ProteomicsIsoleucyl-tRNA synthetase interactome
Aminoacyl-tRNA synthetases are key enzymes in protein synthesis, as they catalyze the attachment of amino acids to their designated, cognate tRNAs. As such, mutations in aminoacyl-tRNA synthetases are associated with severe diseases, such as neurodevelopmental disorders. Many of these mutations fall...
ORGANISM(S): Homo sapiens (Human) 
2026-03-02 | PXD067475 | Pride
Trna Interactome 
ProteomicsCharacterizing the interactome of human Arginyl-tRNA Synthethase
Prior work revealed nuclear-localized aminoacyl-tRNA synthetases (aaRSs) that checked newly synthesized tRNAs for charging before export to the cytoplasm. To reveal other functions, we sought to identify nuclear proteins that interact with arginyl-tRNA synthetase (ArgRS) in the nucleus. Serine/Arg...
ORGANISM(S): Homo sapiens (Human) 
2023-04-14 | PXD015692 | Pride
Arginine Trna syntethase Trna 
ProteomicsMHCI peptidome of HepG2 with ArgRS or SRRM2 knock down
Cells respond to perturbations like inflammation by sensing changes in metabolite levels. Especially prominent is arginine, which has known connections to the inflammatory response. Here, we found that depletion of arginine during inflammation decreased levels of a nuclear form of arginyl-tRNA synth...
ORGANISM(S): Homo sapiens (Human) 
2023-04-14 | PXD036232 | Pride
Inflammation Mhci Peptidome 
ProteomicsN-terminomics upon Arginyl-tRNA synthetase knock down
Arginine is associated with inflammation, cancer, and amino acid signaling, in part through the mTORC1 pathway. In cell-based assays and in the mouse, we found that arginine regulates nuclear levels of arginyl-tRNA synthetase (ArgRS), and that arginine depletion and inflammation reduced nuclear ArgR...
ORGANISM(S): Homo sapiens (Human) 
2023-04-14 | PXD024091 | Pride
Trna Aminoacyl-trna synthetase Splicing N-terminomics 
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