The PARK2/Parkin receptor on damaged mitochondria revisited-uncovering the role of phosphorylated ubiquitin chains

Noriyuki Matsuda; Keiji Tanaka

doi:10.1080/15548627.2015.1071760

The PARK2/Parkin receptor on damaged mitochondria revisited-uncovering the role of phosphorylated ubiquitin chains

Autophagy. 2015;11(9):1700-1. doi: 10.1080/15548627.2015.1071760.

Authors

Noriyuki Matsuda^{1

2}, Keiji Tanaka³

Affiliations

¹ a Ubiquitin Project; Tokyo Metropolitan Institute of Medical Science ; Setagaya-ku , Tokyo.
² b JST; PRESTO ; Kawaguchi , Saitama , Japan.
³ c Laboratory of Protein Metabolism; Tokyo Metropolitan Institute of Medical Science ; Setagaya-ku , Tokyo , Japan.

Abstract

Phosphorylated ubiquitin produced by PINK1 kinase functions as a PARK2/Parkin activator by derepressing intramolecular autoinhibition of PARK2 E3 activity. Unexpectedly, we revealed that phosphorylated polyubiquitin chain also functions in the PARK2 recruitment process as a PARK2 receptor. Phosphorylated ubiquitin enables us to comprehensively understand how PINK1 and PARK2 catalyzes (phospho-)ubiquitination of depolarized mitochondria and subsequent mitophagy.

Keywords: PARK2 receptor; PARK2/Parkin; PINK1; mitochondria; phosphorylated ubiquitin.

MeSH terms

Mitochondria / metabolism*
Mitophagy*
Models, Biological
Phosphorylation
Ubiquitin / metabolism*
Ubiquitin-Protein Ligases / metabolism*

Substances

Ubiquitin
Ubiquitin-Protein Ligases
parkin protein