USP14 inhibition corrects an in vivo model of impaired mitophagy

ABSTRACT: Mitochondrial autophagy or mitophagy is a key process that allows selective sequestration and degradation of dysfunctional mitochondria to prevent excessive reactive oxygen species, and activation of cell death. Recent studies revealed that ubiquitin proteasome complex activity and mitochondrial membrane rupture are key steps preceding mitophagy, in combination with the ubiquitination of specific outer mitochondrial membrane proteins. The deubiquitinating enzyme ubiquitin specific peptidase 14 (USP14) has been shown to modulate both proteasome activity and autophagy. Here, we report that genetic and pharmacological inhibition of USP14 promotes mitophagy, which occurs in the absence of the well-characterized mediators of mitophagy, PINK1 and Parkin. Critical to USP14-induced mitophagy is th

SUBMITTER: Dr. Elena Ziviani 

PROVIDER: S-SCDT-EMM-2018-09014 | biostudies-other |

REPOSITORIES: biostudies-other