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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
In this Chinese Han population a novel Charcot-Marie-Tooth disease-associated gene mutations of GARS (c.794C>T) was discovered.
At the active site, a glycyl-AMP molecule is synthesized and is waiting for the transfer of the glycyl moiety to occur.
GlyRS functions as a chaperone that critically supports neddylation.
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.
one of the mRNAs isoforms tightly controls expression and localization of human GARS.
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.
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.
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.
Expression of three CMT-mutant GARS proteins in Drosophila induces defects in motor performance and motor and sensory neuron morphology, and shortens lifespan.
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.
we propose that the disease-causing L129P mutant of glycyl-tRNA synthetase is linked to a distribution defect in peripheral nerves in vivo.
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.
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.
We developed an ELISA to detect anti-glycyl-tRNA synthetase by using recombinant protein
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.
we believe that these two novel GARS mutations are the underlying causes of the distal hereditary motor neuropathy type V phenotype
GRS bound to different ERK-activated tumor cells, and released phosphatase 2A (PP2A) from CDH6.
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.
No pathogenic mutations were found, excluding the role of GARS gene as a possible factor in the aetiology of Hirayama disease in this cohort
Gars mutations are associated with Charcot-Marie-Tooth disease type 2D.
Results link the aberrant GlyRS-HDAC6 interaction to Charcot-Marie-Tooth disease type 2D pathology and suggest HDAC6 as an effective therapeutic target.
findings link the selective pathology of Charcot-Marie-Tooth disease type 2D to the neomorphic binding activity of GlyRS(CMT2D) that antagonizes the VEGF-Nrp1 interaction, meaning the VEGF-Nrp1 signalling axis is an actionable target for treating CMT2D
These results suggest that this animal model of CMT using an adenovirus may provide information regarding CMT as well as a useful strategy for the treatment of neuropathic pain.
Results indicate that Charcot-Marie-Tooth peripheral neuropathies, type 2D (CMT2D) phenotype is caused by novel pathogenic roles for the mutant GARS that specifically affect peripheral neurons.
a glycyl-tRNA synthetase (GARS) mutation causes peripheral sensory and motor phenotypes creating a model of Charcot-Marie-Tooth type 2D peripheral neuropathy
Gars(C201R) mutation significantly delayed disease onset in the SOD1(G93A);Gars(C201R/+) double heterozygous mutant mice and increased lifespan by 29% on the genetic background investigated
Expression levels of ADSL, GARS-AIRS-GART, and DGAT1 were higher in longissimus lumborum muscle than in heart or liver tissues
This gene encodes glycyl-tRNA synthetase, one of the aminoacyl-tRNA synthetases that charge tRNAs with their cognate amino acids. The encoded enzyme is an (alpha)2 dimer which belongs to the class II family of tRNA synthetases. It has been shown to be a target of autoantibodies in the human autoimmune diseases, polymyositis or dermatomyositis.
, Charcot-Marie-Tooth neuropathy 2D
, Charcot-Marie-Tooth neuropathy, neuronal type, D
, diadenosine tetraphosphate synthetase
, glycine tRNA ligase
, glycine--tRNA ligase
, glycyl-tRNA synthetase
, storage granule protein 23
, glycyl-tran synthetase