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Immunol."],"abstract":"<jats:p>Anti-synthetase syndrome (ASSD) is an autoimmune disease characterized by the presence of autoantibodies targeting one of several aminoacyl t-RNA synthetases (aaRSs) along with clinical features including interstitial lung disease, myositis, Raynaud\u2019s phenomenon, arthritis, mechanic\u2019s hands, and fever. The family of aaRSs consists of highly conserved cytoplasmic and mitochondrial enzymes, one for each amino acid, which are essential for the RNA translation machinery and protein synthesis. Along with their main functions, aaRSs are involved in the development of immune responses, regulation of transcription, and gene-specific silencing of translation. During the last decade, these proteins have been associated with cancer, neurological disorders, infectious responses, and autoimmune diseases including ASSD. To date, several aaRSs have been described to be possible autoantigens in different diseases. The most commonly described are histidyl (HisRS), threonyl (ThrRS), alanyl (AlaRS), glycyl (GlyRS), isoleucyl (IleRS), asparaginyl (AsnRS), phenylalanyl (PheRS), tyrosyl (TyrRS), lysyl (LysRS), glutaminyl (GlnRS), tryptophanyl (TrpRS), and seryl (SerRS) tRNA synthetases. Autoantibodies against the first eight autoantigens listed above have been associated with ASSD while the rest have been associated with other diseases. This review will address what is known about the function of the aaRSs with a focus on their autoantigenic properties. We will also describe the anti-aaRSs autoantibodies and their association to specific clinical manifestations, and discuss their potential contribution to the pathogenesis of ASSD.<\/jats:p>","DOI":"10.3389\/fimmu.2022.866087","type":"journal-article","created":{"date-parts":[[2022,5,13]],"date-time":"2022-05-13T05:57:15Z","timestamp":1652421435000},"update-policy":"https:\/\/doi.org\/10.3389\/crossmark-policy","source":"Crossref","is-referenced-by-count":87,"title":["Aminoacyl-tRNA Synthetases: On Anti-Synthetase Syndrome and Beyond"],"prefix":"10.3389","volume":"13","author":[{"given":"Angeles S.","family":"Galindo-Feria","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Antonella","family":"Notarnicola","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ingrid E.","family":"Lundberg","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Begum","family":"Horuluoglu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1965","published-online":{"date-parts":[[2022,5,13]]},"reference":[{"key":"B1","doi-asserted-by":"publisher","DOI":"10.1097\/CPM.0000000000000171","article-title":"The Diagnosis and Treatment of Antisynthetase Syndrome","volume":"23","author":"Witt","year":"2016","journal-title":"Clin Pulm Med"},{"key":"B2","doi-asserted-by":"publisher","DOI":"10.1378\/chest.10-0180","article-title":"Interstitial Lung Disease Associated With the Idiopathic Inflammatory Myopathies: What Progress has Been Made in the Past 35 Years","volume":"138","author":"Connors","year":"2010","journal-title":"Chest"},{"key":"B3","article-title":"New Insights Into Antisynthetase Syndrome","volume":"11","author":"Cojocaru","year":"2016","journal-title":"Maedica (Bucur)"},{"key":"B4","doi-asserted-by":"publisher","DOI":"10.1016\/j.autrev.2012.06.006","article-title":"Hierarchical Cluster and Survival Analyses of Antisynthetase Syndrome: Phenotype and Outcome Are Correlated With Anti-tRNA Synthetase Antibody Specificity","volume":"12","author":"Hervier","year":"2012","journal-title":"Autoimmun Rev"},{"key":"B5","doi-asserted-by":"publisher","DOI":"10.1002\/acr.21895","article-title":"Interstitial Lung Disease in Anti-Jo-1 Patients With Antisynthetase Syndrome","volume":"65","author":"Marie","year":"2013","journal-title":"Arthritis Care Res (Hoboken)"},{"key":"B6","doi-asserted-by":"publisher","DOI":"10.1016\/j.ijbiomac.2017.12.157","article-title":"Aminoacyl-tRNA Synthetases: Structure, Function, and Drug Discovery","volume":"111","author":"Rajendran","year":"2018","journal-title":"Int J Biol Macromol"},{"key":"B7","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.bi.56.070187.001013","article-title":"Aminoacyl tRNA Synthetases: General Scheme of Structure-Function Relationships in the Polypeptides and Recognition of Transfer RNAs","volume":"56","author":"Schimmel","year":"1987","journal-title":"Annu Rev Biochem"},{"key":"B8","doi-asserted-by":"publisher","first-page":"277","DOI":"10.1016\/bs.enz.2020.06.009","article-title":"Human Diseases Linked to Cytoplasmic aminoacyl-tRNA Synthetases","volume":"48","author":"Jiang","year":"2020","journal-title":"Enzymes"},{"key":"B9","doi-asserted-by":"publisher","DOI":"10.1038\/304177a0","article-title":"Myositis Autoantibody Inhibits histidyl-tRNA Synthetase: A Model for Autoimmunity","volume":"304","author":"Mathews","year":"1983","journal-title":"Nature"},{"key":"B10","doi-asserted-by":"publisher","DOI":"10.1002\/art.1780230802","article-title":"Heterogeneity of Precipitating Antibodies in Polymyositis and Dermatomyositis. 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