PARK15/FBXO7 is dispensable for PINK1/Parkin mitophagy in iNeurons and HeLa cell systems.

ABSTRACT: The protein kinase PINK1 and ubiquitin ligase Parkin promote removal of damaged mitochondria via a feed-forward mechanism involving ubiquitin (Ub) phosphorylation (pUb), Parkin activation, and ubiquitylation of mitochondrial outer membrane proteins to support the recruitment of mitophagy receptors. The ubiquitin ligase substrate receptor FBXO7/PARK15 is mutated in an early-onset parkinsonian-pyramidal syndrome. Previous studies have proposed a role for FBXO7 in promoting Parkin-dependent mitophagy. Here, we systematically examine the involvement of FBXO7 in depolarization and ^mt UPR-dependent mitophagy in the well-established HeLa and induced-neurons cell systems. We find that FBXO7^-/- cells have no demonstrable defect in: (i) kinetics of pUb accumulation, (ii) pUb pu

SUBMITTER: Kraus F 

PROVIDER: S-EPMC10398645 | biostudies-literature | 2023 Aug

REPOSITORIES: biostudies-literature