Mammalian aminoacyl-tRNA synthetases: cell signaling functions of the protein translation machinery
- PMID: 19962454
- DOI: 10.1016/j.vph.2009.11.009
Mammalian aminoacyl-tRNA synthetases: cell signaling functions of the protein translation machinery
Abstract
Aminoacyl-tRNA synthetases (aaRSs) are enzymes that join amino acids to tRNAs. Although they are housekeeping enzymes essential for protein synthesis, aaRSs are now known to participate in a wide variety of functions, including transcription, translation, splicing, inflammation, angiogenesis and apoptosis. In eukaryotes, the functional expansion of aaRSs is closely linked to evolutionary advantages conferred by recruitment into protein complexes as well as various structural adaptations. The elucidation and understanding of the diverse functions of aaRSs is a major goal of current and future research. These investigations will undoubtedly provide some of the most fundamental understanding of how and possibly why synthetases became so tightly involved in such a vast array of cell signaling pathways.
2009 Elsevier Inc. All rights reserved.
Similar articles
-
Functional expansion of aminoacyl-tRNA synthetases and their interacting factors: new perspectives on housekeepers.Trends Biochem Sci. 2005 Oct;30(10):569-74. doi: 10.1016/j.tibs.2005.08.004. Trends Biochem Sci. 2005. PMID: 16125937 Review.
-
Non-canonical functions of aminoacyl-tRNA synthetases.Biochemistry (Mosc). 2000 Aug;65(8):888-97. Biochemistry (Mosc). 2000. PMID: 11002181 Review.
-
Handling mammalian mitochondrial tRNAs and aminoacyl-tRNA synthetases for functional and structural characterization.Methods. 2008 Feb;44(2):176-89. doi: 10.1016/j.ymeth.2007.11.002. Methods. 2008. PMID: 18241799
-
[Functional and evolutionary aspects of the aminoacyl-tRNA synthetases].Rev Latinoam Microbiol. 1991 Jan-Mar;33(1):87-101. Rev Latinoam Microbiol. 1991. PMID: 1727028 Review. Spanish.
-
Role of aminoacyl-tRNA synthetases in infectious diseases and targets for therapeutic development.Top Curr Chem. 2014;344:293-329. doi: 10.1007/128_2013_425. Top Curr Chem. 2014. PMID: 23666077 Review.
Cited by
-
let-65 is cytoplasmic methionyl tRNA synthetase in C. elegans.Meta Gene. 2014 Nov 9;2:819-30. doi: 10.1016/j.mgene.2014.08.006. eCollection 2014 Dec. Meta Gene. 2014. PMID: 25606464 Free PMC article.
-
Responses of retinal and brain microvasculature to streptozotocin induced diabetes revealed by global expression profiling.Diab Vasc Dis Res. 2023 Jan-Feb;20(1):14791641221147533. doi: 10.1177/14791641221147533. Diab Vasc Dis Res. 2023. PMID: 36606460 Free PMC article.
-
Domain collapse and active site ablation generate a widespread animal mitochondrial seryl-tRNA synthetase.Nucleic Acids Res. 2023 Oct 13;51(18):10001-10010. doi: 10.1093/nar/gkad696. Nucleic Acids Res. 2023. PMID: 37638745 Free PMC article.
-
Unique domain appended to vertebrate tRNA synthetase is essential for vascular development.Nat Commun. 2012 Feb 21;3:681. doi: 10.1038/ncomms1686. Nat Commun. 2012. PMID: 22353712 Free PMC article.
-
Eukaryotic initiation factor 6 regulates mechanical responses in endothelial cells.J Cell Biol. 2022 Feb 7;221(2):e202005213. doi: 10.1083/jcb.202005213. Epub 2022 Jan 13. J Cell Biol. 2022. PMID: 35024764 Free PMC article.
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources
Other Literature Sources