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FEBS J. 2015 Jan;282(2):215-23. doi: 10.1111/febs.13127. Epub 2014 Nov 20.

PINK1 and Parkin – mitochondrial interplay between phosphorylation and ubiquitylation in Parkinson's disease.

Author information

1
MRC Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, UK.

Abstract

The discovery of mutations in genes encoding protein kinase PTEN-induced kinase 1 (PINK1) and E3 ubiquitin ligase Parkin in familial Parkinson's disease and their association with mitochondria provides compelling evidence that mitochondrial dysfunction is a major contributor to neurodegeneration in Parkinson's disease. In recent years, tremendous progress has been made in the understanding of how PINK1 and Parkin enzymes are regulated and how they influence downstream mitochondrial signalling processes. We provide a critical overview of the key advances in the field and also discuss the outstanding questions, including novel ways in which this knowledge could be exploited to develop therapies against Parkinson's disease.

KEYWORDS:

PINK1; Parkinson's disease; kinase; mitochondria; parkin; ubiquitin

PMID:
25345844
PMCID:
PMC4368378
DOI:
10.1111/febs.13127
[Indexed for MEDLINE]
Free PMC Article

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