Regulation of Parkin E3 ubiquitin ligase activity |
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Authors: | Helen Walden R Julio Martinez-Torres |
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Institution: | Protein Structure and Function Laboratory, London Research Institute of Cancer Research UK, Lincoln's Inn Fields Laboratories, London, UK, Helen.Walden@cancer.org.uk. |
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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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