Anti-GARS antibody - C-terminal

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

Glycyl-tRNA synthetase (GARS) also known as GlyRS is an enzyme involved in the protein synthesis process. GARS catalyzes the attachment of glycine to its corresponding transfer RNA (tRNA) enabling the correct integration of glycine into proteins during translation. It has a molecular mass of approximately 79 kDa and is ubiquitously expressed in many tissues including muscle and the nervous system. The enzyme plays a critical function by ensuring the accurate translation of the genetic code into functional proteins.

Biological function summary

GARS maintains the fidelity of protein synthesis ensuring that glycine gets incorporated into proteins correctly. As part of the aminoacyl-tRNA synthetase family it operates within a larger complex important for cellular protein production. GARS ensures that proteins maintain their proper structure and function by providing the correct amino acids during synthesis. Its activity supports cell survival and proper cellular functions across various tissues.

Pathways

The function of GARS is central in aminoacyl-tRNA biosynthesis and the broader protein synthesis pathway. This enzyme works closely with other aminoacyl-tRNA synthetases to ensure the fidelity of protein translation. Interactions with proteins such as EPRS (glutamyl-prolyl-tRNA synthetase) highlight the coordinated effort among different synthetases for efficient protein biosynthesis linking it to a fundamental cellular process essential for cellular viability and function.

Associated diseases and disorders

Mutations in GARS have been associated with Charcot-Marie-Tooth disease type 2D and distal hereditary motor neuropathy type V. These genetic disorders result in peripheral neuropathy characterized by muscle weakness and sensory deficits. Mutated GARS disrupts normal glycine-tRNA ligation impacting neuronal function. These conditions often involve interactions with proteins like neurofilament proteins contributing to neurodegeneration.