Tollip coordinates Parkin-dependent trafficking of mitochondria-derived vesicles

ABSTRACT: Multiple mitochondrial quality control pathways exist to maintain the health of mitochondria and ensure cell homeostasis. Here we investigate the role of the endosomal adaptor Tollip during mitochondrial stress response and identify its interaction and colocalisation with the Parkinson's disease associated E3 ubiquitin ligase Parkin. The interaction between Tollip and Parkin is dependent on the ubiquitin-binding CUE domain of Tollip, but independent of Tom1 and mitophagy. Interestingly, this interaction is independent of Parkin mitochondrial recruitment and ligase activity but requires an intact Ubiquitin-like (UBL) domain. Importantly, Tollip regulates Parkin-dependent endocytic trafficking of a discrete subset of mitochondria-derived vesicles to facilitate their lysosomal disposal. Retro

SUBMITTER: Dr. Thomas, A Ryan 

PROVIDER: S-SCDT-EMBOJ-2019-102539 | biostudies-other |

REPOSITORIES: biostudies-other