Searching for non-canonical functions of aminoacyl-tRNA synthases based on mutations carried by Charcot-Marie-Tooth patients

Abstract

Charcot-Marie-Tooth (CMT) is a genetic, incurable neurodegenerative disease which etiology is linked to mutations in almost hundred different genes. The disease affects peripheral nerves which control muscle work and their myelin sheath resulting in progressive muscular dystrophy. The most remarkable genes which mutations are associated with CMT phenotype, are genes encoding aminoacyl-tRNA synthases (aaRS). These proteins are enzymes which common role is to catalyze the reaction of amino acids transfer into tRNA molecules and thereby, to participate in translation of genetic code into the language of proteins. aaRS have been gaining new functions resulting from the mutations acquired in the course of evolution. These functions remain unidentified, despite unraveling the binding partners of aaRS. However, the ongoing molecular studies, which focus on mutations carried by CMT patients and model organisms, bring the researchers closer to unravel the novel functions of aaRS and their potential key role in CMT pathogenesis.