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)
Full text not currently available from Enlighten.
Abstract
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 |
---|---|
Status: | Published |
Refereed: | Yes |
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 |
Publisher: | Springer |
ISSN: | 1420-682X |
ISSN (Online): | 1420-9071 |
Published Online: | 19 April 2012 |
University Staff: Request a correction | Enlighten Editors: Update this record