Jin-Mi Heo

TL;DR: A self-reinforcing positive feedback mechanism is revealed that coordinates TBK1-dependent autophagy adaptor phosphorylation with the assembly of ubiquitin chains on mitochondria to facilitate efficient mitophagy, and mechanistically links genes mutated in Parkinson's disease and amyotrophic lateral sclerosis in a common selective Autophagy pathway.

TL;DR: In this paper, the PINK1 kinase-PARKIN UB ligase mitochondrial control pathway disrupted in Parkinson's disease was dissected using quantitative proteomics and live-cell imaging, revealing a feed forward mechanism that explains how PARKIN phosphorylation of both PARKIN and poly-UB chains synthesized by PARKIN drives a program of PARKIN recruitment and mitochondrial ubiquitylation.

TL;DR: This Review discusses the biochemical steps and regulatory mechanisms that promote the conjugation of ubiquitin to damaged mitochondria via the PTEN-induced putative kinase 1 (PINK1) and the E3 Ubiquitin-protein ligase parkin and how ubiquitIn chains promote autophagosomal capture.

TL;DR: It is demonstrated that Ydr049 (renamed VCP/Cdc48-associated mitochondrial stress-responsive--Vms1), a member of an unstudied pan-eukaryotic protein family, translocates from the cytosol to mitochondria upon mitochondrial stress.

TL;DR: A UB replacement system is used to elucidate steps in the pathway that require PARKIN and/or UB phosphorylation by PINK1 and provide evidence of a Pink1- and UB-driven feed-forward mechanism important for efficient mitochondrial ubiquitylation and mitophagy.