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Regulation of Parkin E3 ubiquitin ligase activity

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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.

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Acknowledgment

This work was supported by Cancer Research UK. H.W. is a European Molecular Biology Organisation (EMBO) Young Investigator.

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  1. Protein Structure and Function Laboratory, London Research Institute of Cancer Research UK, Lincoln’s Inn Fields Laboratories, London, UK

    Helen Walden & R. Julio Martinez-Torres

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  1. Helen Walden
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  2. R. Julio Martinez-Torres
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Correspondence to Helen Walden.

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Walden, H., Martinez-Torres, R.J. Regulation of Parkin E3 ubiquitin ligase activity. Cell. Mol. Life Sci. 69, 3053–3067 (2012). https://doi.org/10.1007/s00018-012-0978-5

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