PINK1-PARKIN interplay: down to ubiquitin phosphorylation

Alexandra Stolz; Ivan Dikic

doi:10.1016/j.molcel.2014.10.022

PINK1-PARKIN interplay: down to ubiquitin phosphorylation

Mol Cell. 2014 Nov 6;56(3):341-342. doi: 10.1016/j.molcel.2014.10.022. Epub 2014 Nov 6.

Authors

Alexandra Stolz¹, Ivan Dikic²

Affiliations

¹ Institute of Biochemistry II, Goethe University, Theodor-Stern-Kai 7, 60590 Frankfurt am Main, Germany.
² Institute of Biochemistry II, Goethe University, Theodor-Stern-Kai 7, 60590 Frankfurt am Main, Germany; Buchmann Institute for Molecular Life Sciences, Max-von-Laue-Strasse 15, 60438 Frankfurt am Main, Germany. Electronic address: ivan.dikic@biochem2.de.

PMID: 25514179
DOI: 10.1016/j.molcel.2014.10.022

Abstract

By using quantitative proteomics, Ordureau et al. (2014) provide a comprehensive view on the regulatory steps by which PINK1-mediated phosphorylation of PARKIN and ubiquitin triggers the recruitment of the ubiquitin ligase PARKIN to damaged mitochondria.

Publication types

Comment

MeSH terms

Humans
Mitochondria / enzymology*
Polyubiquitin / biosynthesis*
Ubiquitin-Protein Ligases / metabolism*
Ubiquitination*

Substances

Polyubiquitin
Ubiquitin-Protein Ligases
parkin protein