Lon protease inactivation in Drosophila causes unfolded protein stress and inhibition of mitochondrial translation.

ABSTRACT: Mitochondrial dysfunction is a frequent participant in common diseases and a principal suspect in aging. To combat mitochondrial dysfunction, eukaryotes have evolved a large repertoire of quality control mechanisms. One such mechanism involves the selective degradation of damaged or misfolded mitochondrial proteins by mitochondrial resident proteases, including proteases of the ATPase Associated with diverse cellular Activities (AAA⁺) family. The importance of the AAA⁺ family of mitochondrial proteases is exemplified by the fact that mutations that impair their functions cause a variety of human diseases, yet our knowledge of the cellular responses to their inactivation is limited. To address this matter, we created and characterized flies with complete or partial ina

SUBMITTER: Pareek G 

PROVIDER: S-EPMC6197249 | biostudies-literature | 2018

REPOSITORIES: biostudies-literature