Human Glycyl-tRNA synthetase(GARS) ELISA kit

Catalyzes the ATP-dependent ligation of glycine to the 3'-end of its cognate tRNA, via the formation of an aminoacyl-adenylate intermediate (Gly-AMP). Also produces diadenosine tetraphosphate (Ap4A), a universal pleiotropic signaling molecule needed for cell regulation pathways, by direct condensation of 2 ATPs. Thereby, may play a special role in Ap4A homeostasis.

1. In support of GARS variant pathogenicity, our patient shows striking phenotypic overlap with other patients having ARS-related recessive diseases; this observation is consistent with the essential function of GARS in both cellular locations. In summary, our clinical, genetic, and functional analyses expand the phenotypic spectrum associated with GARS variants PMID: 28675565
2. In this Chinese Han population a novel Charcot-Marie-Tooth disease-associated gene mutations of GARS (c.794C>T) was discovered. PMID: 27862672
3. At the active site, a glycyl-AMP molecule is synthesized and is waiting for the transfer of the glycyl moiety to occur. PMID: 27261259
4. GlyRS functions as a chaperone that critically supports neddylation. PMID: 27348078
5. Data indicate that dimerization is required for the dominant neurotoxicity of disease-associated GARS mutations and provide a rapid, tractable model for studying newly identified GARS variants for a role in human disease. PMID: 27008886
6. one of the mRNAs isoforms tightly controls expression and localization of human GARS. PMID: 26327585
7. This study reports two crystal structures of human GlyRS variants, in the free form and in complex with tRNA(Gly) respectively, and reveal new aspects of the glycylation mechanism. PMID: 26797133
8. GARS mutations are an uncommon cause of Charcot-Marie-Tooth Disease (CMT) in Taiwan. The p.Asp146Tyr and p.Met238Arg mutations are associated with early-onset axonal CMT. PMID: 26244500
9. Our findings suggest that mutant GlyRS gains access to ectopic sub-compartments of the motor neuron, providing a possible explanation for the selective neuropathology caused by mutations in a widely expressed gene. PMID: 25972375
10. Expression of three CMT-mutant GARS proteins in Drosophila induces defects in motor performance and motor and sensory neuron morphology, and shortens lifespan. PMID: 26138142
11. The c.999G>T mutation is a novel mutation of the glycyl-tRNA synthetase gene that has not been previously reported. The phenotype of this family is Charcot-Marie-Tooth disease type 2D, which is first reported in Chinese population. PMID: 26000875
12. we propose that the disease-causing L129P mutant of glycyl-tRNA synthetase is linked to a distribution defect in peripheral nerves in vivo. PMID: 25218976
13. our data indicate that impaired function is a key component of GARS-mediated CMT disease and emphasize the need for careful genetic and functional evaluation before implicating a variant in disease onset. PMID: 25168514
14. 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. PMID: 24807208
15. We developed an ELISA to detect anti-glycyl-tRNA synthetase by using recombinant protein PMID: 24508626
16. Report crystal structures of wild type and mutant GlyRS in complex with tRNA and with small substrates and describe the molecular details of enzymatic recognition of the key tRNA identity elements in the acceptor stem and the anticodon loop. PMID: 24898252
17. we believe that these two novel GARS mutations are the underlying causes of the distal hereditary motor neuropathy type V phenotype PMID: 23279345
18. GRS bound to different ERK-activated tumor cells, and released phosphatase 2A (PP2A) from CDH6. PMID: 22345558
19. missense mutations of Gars may cause some loss of function, the dominant neuropathy phenotype observed in mice is caused by a dose-dependent gain of function that is not mitigated by over-expression of functional wild-type protein. PMID: 22144914
20. No pathogenic mutations were found, excluding the role of GARS gene as a possible factor in the aetiology of Hirayama disease in this cohort PMID: 19412816
21. GARS mutation is a rare cause of Charcot-Marie-Tooth neuropathy among Japanese patients. PMID: 19329989
22. Four disease-associated missense mutations in the glycyl tRNA synthetase gene in families with Charcot-Marie-Tooth disease type 2D and distal spinal muscular atrophy type V PMID: 12690580
23. A novel heterozygous missense GARS gene mutation (D500N) was identified in members of a family affected byCharcot-Marie-Tooth type 2D. PMID: 16534118
24. We screened 100 patients with inherited and sporadic lower motor neuron degeneration and identified three novel missense mutations in the glycyl-tRNA synthetase (GARS) gene. PMID: 17101916
25. The crystal belonged to space group P4(3)2(1)2 or its enantiomorphic space group P4(1)2(1)2, & diffracted X-rays to 3.0 A resolution. The asymmetric unit contained 1 GlyRS molecule & had a solvent content of 69%. PMID: 17142907
26. Crystal structure of human wildtype and S581L-mutant glycyl-tRNA synthetase. PMID: 17544401
27. The structure of wild type and Charcot-Marie-Tooth-causing mutant of homodimeric GlyRS are reported. PMID: 17545306
28. Charcot-Marie-Tooth (CMT) disease-causing mutations of glycine-tRNA synthetase share a common defect in localization which may be connected to a change in surfaces at the dimer interface, and may cause a dominant axonal form of CMT (type 2D). PMID: 17595294
29. we present a comparison between the crystal structures of the eubacterial Escherichia coli and the human tRNA(Gly) acceptor stem microhelices and their surrounding hydration patterns. PMID: 18275849
30. human glycyl-tRNA synthetase has a role in Ap4A homeostasis PMID: 19710017

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Charcot-Marie-Tooth disease 2D (CMT2D); Neuronopathy, distal hereditary motor, 5A (HMN5A)

Cytoplasm. Cell projection, axon. Secreted. Secreted, extracellular exosome.; [Isoform 1]: Mitochondrion. Cytoplasm.; [Isoform 2]: Cytoplasm. Cell projection, axon.

Class-II aminoacyl-tRNA synthetase family

Widely expressed, including in brain and spinal cord.; [Isoform 2]: Expressed in brain, spinal cord, muscle, heart and spleen.; [Isoform 1]: Expressed in brain, spinal cord, muscle, heart, spleen and liver.

HGNC: 4162

OMIM: 600287

KEGG: hsa:2617

STRING: 9606.ENSP00000373918

UniGene: Hs.404321