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Cell Mol Life Sci. 2012 Sep;69(18):3053-67. doi: 10.1007/s00018-012-0978-5. Epub 2012 Apr 19.

Regulation of Parkin E3 ubiquitin ligase activity.

Author information

1
Protein Structure and Function Laboratory, London Research Institute of Cancer Research UK, Lincoln's Inn Fields Laboratories, London, UK. Helen.Walden@cancer.org.uk

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.

PMID:
22527713
DOI:
10.1007/s00018-012-0978-5
[Indexed for MEDLINE]

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