| Tyrosyl-tRNA synthetase has a noncanonical function in actin bundling. | Tyrosyl-tRNA synthetase has a noncanonical function in actin bundling.
Ermanoska B, Asselbergh B, Morant L, Petrovic-Erfurth ML, Hosseinibarkooie S, Leitão-Gonçalves R, Almeida-Souza L, Bervoets S, Sun L, Lee L, Atkinson D, Khanghahi A, Tournev I, Callaerts P, Verstreken P, Yang XL, Wirth B, Rodal AA, Timmerman V, Goode BL, Godenschwege TA, Jordanova A., Free PMC Article | 03/14/2023 |
| The recurrent missense mutation p.(Arg367Trp) in YARS1 causes a distinct neurodevelopmental phenotype. | The recurrent missense mutation p.(Arg367Trp) in YARS1 causes a distinct neurodevelopmental phenotype.
Averdunk L, Sticht H, Surowy H, Lüdecke HJ, Koch-Hogrebe M, Alsaif HS, Kahrizi K, Alzaidan H, Alawam BS, Tohary M, Kraus C, Endele S, Wadman E, Kaplan JD, Efthymiou S, Najmabadi H, Reis A, Alkuraya FS, Wieczorek D., Free PMC Article | 02/26/2022 |
| Novel partial loss-of-function variants in the tyrosyl-tRNA synthetase 1 (YARS1) gene involved in multisystem disease. | Novel partial loss-of-function variants in the tyrosyl-tRNA synthetase 1 (YARS1) gene involved in multisystem disease.
Estève C, Roman C, DeLeusse C, Baravalle M, Bertaux K, Blanc F, Bourgeois P, Bresson V, Cano A, Coste ME, Delteil C, Lacoste C, Loosveld M, De Paula AM, Monnier AS, Secq V, Levy N, Badens C, Fabre A. | 11/13/2021 |
| Moonlighting matrix metalloproteinase substrates: Enhancement of proinflammatory functions of extracellular tyrosyl-tRNA synthetase upon cleavage. | Moonlighting matrix metalloproteinase substrates: Enhancement of proinflammatory functions of extracellular tyrosyl-tRNA synthetase upon cleavage.
Jobin PG, Solis N, Machado Y, Bell PA, Rai SK, Kwon NH, Kim S, Overall CM, Butler GS., Free PMC Article | 10/24/2020 |
| study revealed a new radiation protection mechanism for RSV, in which the acetylation of TyrRS and its translocation into the nucleus is promoted, and this mechanism may also represent a novel protective target against irradiation. | Resveratrol targets TyrRS acetylation to protect against radiation-induced damage.
Gao P, Li N, Ji K, Wang Y, Xu C, Liu Y, Wang Q, Wang J, He N, Sun Z, Du L, Liu Q. | 05/23/2020 |
| By revealing the existence of a YARS-PI3K-Akt signaling axis in gastric cancer, we discovered that tRNA synthetase YARS is a novel tumorigenic factor, characterized by its upregulation in tumor-derived specimens, as well as its functions in promoting gastric cancer progression. | YARS as an oncogenic protein that promotes gastric cancer progression through activating PI3K-Akt signaling.
Zhang C, Lin X, Zhao Q, Wang Y, Jiang F, Ji C, Li Y, Gao J, Li J, Shen L., Free PMC Article | 02/29/2020 |
| Analysis of YARS p.Pro167Thr in yeast complementation assays revealed a loss-of-function, hypomorphic allele that significantly impaired growth. Recombinant YARS p.Pro167Thr demonstrated normal subcellular localization, but greatly diminished ability to homodimerize in human embryonic kidney cells. | Homozygosity for a mutation affecting the catalytic domain of tyrosyl-tRNA synthetase (YARS) causes multisystem disease.
Williams KB, Brigatti KW, Puffenberger EG, Gonzaga-Jauregui C, Griffin LB, Martinez ED, Wenger OK, Yoder MA, Kandula VVR, Fox MD, Demczko MM, Poskitt L, Furuya KN, Reid JG, Overton JD, Baras A, Miles L, Radhakrishnan K, Carson VJ, Antonellis A, Jinks RN, Strauss KA., Free PMC Article | 06/22/2019 |
| conclusion is further supported by a positive correlation across brain regions between TyrRS expression and arginine-accelerated KTP production. | Tyrosyl-tRNA synthetase: A potential kyotorphin synthetase in mammals.
Tsukahara T, Yamagishi S, Neyama H, Ueda H. | 12/29/2018 |
| Platelet replenishment by YRS(ACT) is independent of thrombopoietin (TPO), as evidenced by expansion of the megakaryocytes from induced pluripotent stem cell-derived hematopoietic stem cells from a patient deficient in TPO signaling. | Tyrosyl-tRNA synthetase stimulates thrombopoietin-independent hematopoiesis accelerating recovery from thrombocytopenia.
Kanaji T, Vo MN, Kanaji S, Zarpellon A, Shapiro R, Morodomi Y, Yuzuriha A, Eto K, Belani R, Do MH, Yang XL, Ruggeri ZM, Schimmel P., Free PMC Article | 10/6/2018 |
| These YARS variants occur in the catalytic domain and the C-terminal domain, respectively. Mutations in YARS have been previously associated with an autosomal dominant form of Charcot-Marie-Tooth (CMT); our findings suggest the disease spectrum associated with YARS dysregulation is broader than peripheral neuropathy. | A novel multisystem disease associated with recessive mutations in the tyrosyl-tRNA synthetase (YARS) gene.
Nowaczyk MJ, Huang L, Tarnopolsky M, Schwartzentruber J, Majewski J, Bulman DE, FORGE Canada Consortium, Care4Rare Canada Consortium, Hartley T, Boycott KM. | 10/21/2017 |
| Studied the structural effect of three Charcot-Marie-Tooth disease-causing mutations in tyrosyl-tRNA synthetase. The mutations do not induce changes in protein secondary structures, or shared effects on oligomerization state and stability. However, all mutations provide access to a surface masked in the wild-type enzyme, and that access correlates with protein misinteraction. | Alternative stable conformation capable of protein misinteraction links tRNA synthetase to peripheral neuropathy.
Blocquel D, Li S, Wei N, Daub H, Sajish M, Erfurth ML, Kooi G, Zhou J, Bai G, Schimmel P, Jordanova A, Yang XL., Free PMC Article | 10/14/2017 |
| Data show that the internal deletion of tyrosyl-tRNA synthetase TyrRSDeltaE2-4 splice variants (SVs) gave an alternative, neomorphic dimer interface 'orthogonal' to that of native TyrRS. | Alternative splicing creates two new architectures for human tyrosyl-tRNA synthetase.
Wei Z, Xu Z, Liu X, Lo WS, Ye F, Lau CF, Wang F, Zhou JJ, Nangle LA, Yang XL, Zhang M, Schimmel P., Free PMC Article | 07/16/2016 |
| Expression of CMT-mutant tyrosyl-tRNA synthetase in Drosophila impairs protein translation. | Impaired protein translation in Drosophila models for Charcot-Marie-Tooth neuropathy caused by mutant tRNA synthetases.
Niehues S, Bussmann J, Steffes G, Erdmann I, Köhrer C, Sun L, Wagner M, Schäfer K, Wang G, Koerdt SN, Stum M, Jaiswal S, RajBhandary UL, Thomas U, Aberle H, Burgess RW, Yang XL, Dieterich D, Storkebaum E., Free PMC Article | 04/16/2016 |
| Computational modeling of molecular dynamics of G41R mutant form of human tyrosyl-tRNA synthetase, assosiated with Charcot-Marie-Tooth neuropathy has been presented. | [COMPUTATIONAL MODELING OF MOLECULAR DYNAMICS OF G41R MUTANT FORM OF HUMAN TYROSYL-tRNA SYNTHETASE, ASSOSIATED WITH CHARCOT-MARIE-TOOTH NEUROPATHY].
Savytskyi OV, Kornelyuk AI. | 04/9/2016 |
| the association of rare YARS variant with late-onset autosomal dominant Charcot-Marie-Tooth neuropathy | Rare variants in methionyl- and tyrosyl-tRNA synthetase genes in late-onset autosomal dominant Charcot-Marie-Tooth neuropathy.
Hyun YS, Park HJ, Heo SH, Yoon BR, Nam SH, Kim SB, Park CI, Choi BO, Chung KW. | 07/25/2015 |
| This study presents genetic evidence for common mutant-specific interactions between two CMT-associated aminoacyl-tRNA synthetases, lending support for a shared mechanism responsible for the synthetase-induced peripheral neuropathies. | CMT-associated mutations in glycyl- and tyrosyl-tRNA synthetases exhibit similar pattern of toxicity and share common genetic modifiers in Drosophila.
Ermanoska B, Motley WW, Leitão-Gonçalves R, Asselbergh B, Lee LH, De Rijk P, Sleegers K, Ooms T, Godenschwege TA, Timmerman V, Fischbeck KH, Jordanova A., Free PMC Article | 05/16/2015 |
| rhTyrRS promotes migration and aggregation of megakaryocytes to the bone marrow niche | Recombinant human tyrosyl-tRNA synthetase, a novel thrombopoietic agent.
Ling Z, Yanling Z, Zhe F, Kui C, Xiushi Z, Min Y, Wei M. | 04/11/2015 |
| nuclear-localized TyrRS activates transcription factor E2F1 to upregulate the expression of DNA damage repair genes such as BRCA1 and RAD51. | Oxidative stress diverts tRNA synthetase to nucleus for protection against DNA damage.
Wei N, Shi Y, Truong LN, Fisch KM, Xu T, Gardiner E, Fu G, Hsu YO, Kishi S, Su AI, Wu X, Yang XL., Free PMC Article | 01/10/2015 |
| A major difference between the first- and second-generation tRNA synthetases (RSs) is that the second-generation RSs have an active site more compatible with tyrosine binding. | Structural basis of improved second-generation 3-nitro-tyrosine tRNA synthetases.
Cooley RB, Feldman JL, Driggers CM, Bundy TA, Stokes AL, Karplus PA, Mehl RA., Free PMC Article | 05/24/2014 |
| The full length tyrosyl-tRNA synthetase lacks its cytokine activity because of the interactions between N-terminal and the C-terminal modules, which protect the ELR cytokine motif. | Asymmetric structure and domain binding interfaces of human tyrosyl-tRNA synthetase studied by molecular dynamics simulations.
Savytskyi OV, Yesylevskyy SO, Kornelyuk AI. | 11/16/2013 |
| Naturally occurring fragments of the two proteins involved in translation, TyrRS and TrpRS, have opposing activities on angiogenesis. | Inhibition of mini-TyrRS-induced angiogenesis response in endothelial cells by VE-cadherin-dependent mini-TrpRS.
Zeng R, Chen YC, Zeng Z, Liu XX, Liu R, Qiang O, Li X. | 07/21/2012 |
| Nuclear import of TyrRS is regulated by tRNA(Tyr). | tRNA-controlled nuclear import of a human tRNA synthetase.
Fu G, Xu T, Shi Y, Wei N, Yang XL., Free PMC Article | 06/16/2012 |
| Dominant Intermediate Charcot-Marie-Tooth disorder is not due to a catalytic defect in tyrosyl-tRNA synthetase. | Dominant Intermediate Charcot-Marie-Tooth disorder is not due to a catalytic defect in tyrosyl-tRNA synthetase.
Froelich CA, First EA. | 10/22/2011 |
| Expression of tyrosyl-tRNA synthetase (YARS) DI-CMTC associated mutations (G41R, E196K,153-156delVKQV)in Drosophila leads to neuronal dysfunction. | Dominant mutations in the tyrosyl-tRNA synthetase gene recapitulate in Drosophila features of human Charcot-Marie-Tooth neuropathy.
Storkebaum E, Leitão-Gonçalves R, Godenschwege T, Nangle L, Mejia M, Bosmans I, Ooms T, Jacobs A, Van Dijck P, Yang XL, Schimmel P, Norga K, Timmerman V, Callaerts P, Jordanova A., Free PMC Article | 09/20/2010 |
| Human tyrosyl-tRNA synthetase, where a catalytic-domain surface helix, next to the active site, was recruited for interleukin-8-like cytokine signaling. | Mutational separation of aminoacylation and cytokine activities of human tyrosyl-tRNA synthetase.
Kapoor M, Otero FJ, Slike BM, Ewalt KL, Yang XL., Free PMC Article | 01/21/2010 |