Article
CMT2N-causing aminoacylation domain mutants enable Nrp1 interaction with AlaRS.
Proceedings of the National Academy of Sciences of the United States of America - 30 Mar 2021
Sun Litao, Wei Na, Kuhle Bernhard, Blocquel David, Novick Scott, Matuszek Zaneta, Zhou Huihao, He Weiwei, Zhang Jingjing, Weber Thomas, Horvath Rita, Latour Philippe, Pan Tao, Schimmel Paul, Griffin Patrick R, Yang Xiang-Lei
Abstract excerpt
Through dominant mutations, aminoacyl-tRNA synthetases constitute the largest protein family linked to Charcot-Marie-Tooth disease (CMT). An example is CMT subtype 2N (CMT2N), caused by individual mutations spread out in AlaRS, including three in the aminoacylation domain, thereby suggesting a role for a tRNA-charging defect. However, here we found that two are aminoacylation defective but that the most widely...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.