Ermanoska B, Motley WW, Leitão-Gonçalves R, Asselbergh B, Lee LH, De Rijk P, Sleegers K, Ooms T, Godenschwege TA, Timmerman V, Fischbeck KH, Jordanova A. CMT-associated mutations in glycyl- and tyrosyl-tRNA synthetases exhibit similar pattern of toxicity and share common genetic modifiers in Drosophila. Neurobiol Dis. 2014 Aug;68:180-9. PMID: 24807208; PMCID: PMC4086162.
From the abstract: "Aminoacyl-tRNA synthetases are ubiquitously expressed proteins that charge tRNAs with their cognate amino acids. By ensuring the fidelity of protein synthesis, these enzymes are essential for the viability of every cell. Yet, mutations in six tRNA synthetases specifically affect the peripheral nerves and cause Charcot-Marie-Tooth (CMT) disease. ... Our 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. "