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PINK 1 and Parkin – mitochondrial interplay between phosphorylation and ubiquitylation in Parkinson's disease
Author(s) -
Kazlauskaite Agne,
Muqit Miratul M. K.
Publication year - 2015
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.13127
Subject(s) - parkin , parkinson's disease , phosphorylation , pink1 , ubiquitin , microbiology and biotechnology , mitochondrion , disease , neuroscience , biology , genetics , medicine , gene
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.