Regulation of Parkin E3 ubiquitin ligase activity

Walden, H. and Martinez-Torres, R. J. (2012) Regulation of Parkin E3 ubiquitin ligase activity. Cellular and Molecular Life Sciences, 69(18), pp. 3053-3067. (doi: 10.1007/s00018-012-0978-5) (PMID:22527713)

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Parkin is an E3 ubiquitin ligase mutated in autosomal recessive juvenile Parkinson’s disease. In addition, it is a putative tumour suppressor, and has roles outside its enzymatic activity. It is critical for mitochondrial clearance through mitophagy, and is an essential protein in most eukaryotes. As such, it is a tightly controlled protein, regulated through an array of external interactions with multiple proteins, posttranslational modifications including phosphorylation and S-nitrosylation, and self-regulation through internal associations. In this review, we highlight some of the recent studies into Parkin regulation and discuss future challenges for gaining a full molecular understanding of the regulation of Parkin E3 ligase activity.

Item Type:Articles
Glasgow Author(s) Enlighten ID:Walden, Professor Helen
Authors: Walden, H., and Martinez-Torres, R. J.
College/School:College of Medical Veterinary and Life Sciences > School of Molecular Biosciences
Journal Name:Cellular and Molecular Life Sciences
ISSN (Online):1420-9071
Published Online:19 April 2012

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