| The alanyl-tRNA synthetase AARS1 moonlights as a lactyltransferase to promote YAP signaling in gastric cancer. | The alanyl-tRNA synthetase AARS1 moonlights as a lactyltransferase to promote YAP signaling in gastric cancer.
Ju J, Zhang H, Lin M, Yan Z, An L, Cao Z, Geng D, Yue J, Tang Y, Tian L, Chen F, Han Y, Wang W, Zhao S, Jiao S, Zhou Z., Free PMC Article | 06/3/2024 |
| Alanyl-tRNA synthetase, AARS1, is a lactate sensor and lactyltransferase that lactylates p53 and contributes to tumorigenesis. | Alanyl-tRNA synthetase, AARS1, is a lactate sensor and lactyltransferase that lactylates p53 and contributes to tumorigenesis.
Zong Z, Xie F, Wang S, Wu X, Zhang Z, Yang B, Zhou F. | 05/29/2024 |
| A humanized yeast model reveals dominant-negative properties of neuropathy-associated alanyl-tRNA synthetase mutations. | A humanized yeast model reveals dominant-negative properties of neuropathy-associated alanyl-tRNA synthetase mutations.
Meyer-Schuman R, Marte S, Smith TJ, Feely SME, Kennerson M, Nicholson G, Shy ME, Koutmou KS, Antonellis A., Free PMC Article | 06/23/2023 |
| Clinical characteristics and proteome modifications in two Charcot-Marie-Tooth families with the AARS1 Arg326Trp mutation. | Clinical characteristics and proteome modifications in two Charcot-Marie-Tooth families with the AARS1 Arg326Trp mutation.
Høyer H, Busk ØL, Esbensen QY, Røsby O, Hilmarsen HT, Russell MB, Nyman TA, Braathen GJ, Nilsen HL., Free PMC Article | 08/27/2022 |
| Protein instability associated with AARS1 and MARS1 mutations causes trichothiodystrophy. | Protein instability associated with AARS1 and MARS1 mutations causes trichothiodystrophy.
Botta E, Theil AF, Raams A, Caligiuri G, Giachetti S, Bione S, Accadia M, Lombardi A, Smith DEC, Mendes MI, Swagemakers SMA, van der Spek PJ, Salomons GS, Hoeijmakers JHJ, Yesodharan D, Nampoothiri S, Ogi T, Lehmann AR, Orioli D, Vermeulen W., Free PMC Article | 04/2/2022 |
| CMT2N-causing aminoacylation domain mutants enable Nrp1 interaction with AlaRS. | CMT2N-causing aminoacylation domain mutants enable Nrp1 interaction with AlaRS.
Sun L, Wei N, Kuhle B, Blocquel D, Novick S, Matuszek Z, Zhou H, He W, Zhang J, Weber T, Horvath R, Latour P, Pan T, Schimmel P, Griffin PR, Yang XL., Free PMC Article | 10/23/2021 |
| Alanyl-tRNA synthetase 1 (AARS1) gene mutation in a family with intermediate Charcot-Marie-Tooth neuropathy. | Alanyl-tRNA synthetase 1 (AARS1) gene mutation in a family with intermediate Charcot-Marie-Tooth neuropathy.
Lee AJ, Nam DE, Choi YJ, Nam SH, Choi BO, Chung KW. | 02/2/2021 |
| we investigated the effects of the severe infantile-onset cardiomyopathy-associated R592W mutation of hmtAlaRS on the canonical enzymatic activities of hmtAlaRS. Overall, our results provide fundamental information about tRNA recognition and deepen our understanding of translational quality control mechanisms by hmtAlaRS. | The G3-U70-independent tRNA recognition by human mitochondrial alanyl-tRNA synthetase.
Zeng QY, Peng GX, Li G, Zhou JB, Zheng WQ, Xue MQ, Wang ED, Zhou XL., Free PMC Article | 10/12/2019 |
| all three mutations caused a pathological phenotype of neural abnormalities when expressed in zebrafish, while expression of the human wild-type messenger RNA (mRNA) did not. Our data indicate that not only functional null or hypomorphic alleles, but also hypermorphic AARS alleles can cause dominantly inherited axonal Charcot-Marie-Tooth (CMT) disease . | Hypermorphic and hypomorphic AARS alleles in patients with CMT2N expand clinical and molecular heterogeneities.
Weterman MAJ, Kuo M, Kenter SB, Gordillo S, Karjosukarso DW, Takase R, Bronk M, Oprescu S, van Ruissen F, Witteveen RJW, Bienfait HME, Breuning M, Verhamme C, Hou YM, de Visser M, Antonellis A, Baas F., Free PMC Article | 05/18/2019 |
| A large sequence divergence of the C-terminal domain (C-Ala) reshaped C-Ala in a way that changed the global architecture of alanyl-tRNA synthetase (AlaRS). This reshaping removed the role of C-Ala in prokaryotes for docking tRNA and instead repurposed it to form a dimer interface presenting a DNA-binding groove. | Two crystal structures reveal design for repurposing the C-Ala domain of human AlaRS.
Sun L, Song Y, Blocquel D, Yang XL, Schimmel P., Free PMC Article | 04/7/2018 |
| Number of missense mutations in AARS expand the clinical spectrum and provide pheno-genotypic correlations in AARS-related neuropathies. | Genotype/phenotype correlations in AARS-related neuropathy in a cohort of patients from the United Kingdom and Ireland.
Bansagi B, Antoniadi T, Burton-Jones S, Murphy SM, McHugh J, Alexander M, Wells R, Davies J, Hilton-Jones D, Lochmüller H, Chinnery P, Horvath R., Free PMC Article | 06/28/2016 |
| A novel mutation in alanyl-tRNA synthetase causes a mild myeloneuropathy, a novel phenotype for patients with mutations in one of the tRNA synthetase genes. | A novel AARS mutation in a family with dominant myeloneuropathy.
Motley WW, Griffin LB, Mademan I, Baets J, De Vriendt E, De Jonghe P, Antonellis A, Jordanova A, Scherer SS., Free PMC Article | 07/25/2015 |
| Loss-of-function alanyl-tRNA synthetase mutations cause an autosomal-recessive early-onset epileptic encephalopathy with persistent myelination defect. | Loss-of-function alanyl-tRNA synthetase mutations cause an autosomal-recessive early-onset epileptic encephalopathy with persistent myelination defect.
Simons C, Griffin LB, Helman G, Golas G, Pizzino A, Bloom M, Murphy JL, Crawford J, Evans SH, Topper S, Whitehead MT, Schreiber JM, Chapman KA, Tifft C, Lu KB, Gamper H, Shigematsu M, Taft RJ, Antonellis A, Hou YM, Vanderver A., Free PMC Article | 05/30/2015 |
| the pathological consequences of diminished tRNA synthetase editing activity, and thus translational infidelity, are dependent on the cell type and the extent of editing disruption | Deficiencies in tRNA synthetase editing activity cause cardioproteinopathy.
Liu Y, Satz JS, Vo MN, Nangle LA, Schimmel P, Ackerman SL., Free PMC Article | 05/2/2015 |
| in a family with distal hereditary motor neuropathy (dHMN), all 4 affected family members had a heterozygous missense mutation c.2677G>A (p.D893N) of (AARS), not found in the 4 unaffected members and control subjects; conclude AARS mutation caused dHMN in a Chinese family; AARS mutations result in not only a CMT phenotype but also a dHMN phenotype | Alanyl-tRNA synthetase mutation in a family with dominant distal hereditary motor neuropathy.
Zhao Z, Hashiguchi A, Hu J, Sakiyama Y, Okamoto Y, Tokunaga S, Zhu L, Shen H, Takashima H., Free PMC Article | 11/24/2012 |
| Methylation-mediated deamination of a CpG dinucleotide gives rise to the recurrent p.Arg329His alanyl-tRNA synthetase mutation in patients with Charcot-Marie-Tooth disease type 2N (CMT2N). | A recurrent loss-of-function alanyl-tRNA synthetase (AARS) mutation in patients with Charcot-Marie-Tooth disease type 2N (CMT2N).
McLaughlin HM, Sakaguchi R, Giblin W, NISC Comparative Sequencing Program, Wilson TE, Biesecker L, Lupski JR, Talbot K, Vance JM, Züchner S, Lee YC, Kennerson M, Hou YM, Nicholson G, Antonellis A., Free PMC Article | 04/28/2012 |
| We show here that mutations in AARS2 cause perinatal or infantile cardiomyopathy with near-total combined mitochondrial respiratory chain deficiency in the heart. | Exome sequencing identifies mitochondrial alanyl-tRNA synthetase mutations in infantile mitochondrial cardiomyopathy.
Götz A, Tyynismaa H, Euro L, Ellonen P, Hyötyläinen T, Ojala T, Hämäläinen RH, Tommiska J, Raivio T, Oresic M, Karikoski R, Tammela O, Simola KO, Paetau A, Tyni T, Suomalainen A., Free PMC Article | 08/20/2011 |
| cytoplasmic Alanyl-tRNA synthetase may have a role in dominant axonal Charcot-Marie-Tooth disease, as shown by its mutation in a major determinant for binding and aminoacylation | A major determinant for binding and aminoacylation of tRNA(Ala) in cytoplasmic Alanyl-tRNA synthetase is mutated in dominant axonal Charcot-Marie-Tooth disease.
Latour P, Thauvin-Robinet C, Baudelet-Méry C, Soichot P, Cusin V, Faivre L, Locatelli MC, Mayençon M, Sarcey A, Broussolle E, Camu W, David A, Rousson R., Free PMC Article | 03/1/2010 |