Serine--tRNA ligase, cytoplasmic (SARS1)

Serine--tRNA ligase, cytoplasmic (SARS1) is a class II aminoacyl-tRNA synthetase that catalyzes the specific attachment of serine to its corresponding tRNA (tRNA(Ser)), a critical step in protein synthesis[1][3][4]. It also participates in selenocysteine biosynthesis by misacylating tRNA(Sec) with serine, which is later converted to selenocysteine[1]. SARS1 regulates vascular development by modulating VEGFA gene transcription and angiogenesis[1][2]. Mutations in SARS1 are associated with rare genetic syndromes such as neurodevelopmental disorders, arteriovenous malformations in the brain, and HUPRA syndrome[1][2][3]. The enzyme functions primarily as a homodimer and contains catalytic and tRNA-binding domains[3]. While important biologically, SARS1 is not currently a therapeutic target for approved drugs due to the essential nature of its role in protein synthesis and high risk for toxicity if inhibited[1][3].

Other names

SARS1SerRSSERSSeryl-tRNA synthetaseSeryl-tRNA(Ser/Sec) synthetaseSerine-tRNA ligase 1, cytoplasmicSARSSERRSNEDMAS

In theory, drugs targeting SARS1 would likely be inhibitors of the serine-tRNA ligase enzyme, blocking or modulating the aminoacylation of tRNA(Ser) and thus interrupting protein synthesis. However, no established clinical mechanisms or drugs have been described for SARS1 specifically[1][3].