How could Parkin-mediated ubiquitination of mitofusin promote mitophagy?

TitleHow could Parkin-mediated ubiquitination of mitofusin promote mitophagy?
Publication TypeJournal Article
Year of Publication2010
AuthorsZiviani, E, Whitworth, AJ
Date Published2010 Jul
KeywordsAnimals, Drosophila melanogaster, Humans, Mitochondrial Degradation, Mitochondrial Proteins, Models, Biological, Parkinson Disease, Ubiquitin-Protein Ligases, Ubiquitination

Much evidence links mitochondrial dysfunction to the death of neurons in Parkinson disease (PD), and is particularly emphasized by our growing understanding of the function of genes linked to recessively inherited PD such as PINK1, parkin and DJ-1. Recent work has revealed an exciting link between the PINK1-Parkin pathway and the autophagic turnover of dysfunctional mitochondrial (mitophagy). We have recently shown that mitofusin is ubiquitinated by Parkin when it is recruited to dysfunctional mitochondria. Recent work also shows that regulated fission and fusion events help segregate dysfunctional mitochondria prior to mitophagy. Here we hypothesize how Parkin-mediated ubiquitination of Mfn may play a role in this mechanism.

Alternate JournalAutophagy
Citation Key10.4161/auto.6.5.12242
PubMed ID20484985
PubMed Central IDPMC4196639
Grant List089698 / / Wellcome Trust / United Kingdom