title: Regulation of Parkin E3 ubiquitin ligase activity.
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.
authors.affiliation: Protein Structure and Function Laboratory, London Research Institute of Cancer Research UK, Lincoln's Inn Fields Laboratories, London, UK. Helen.Walden@cancer.org.uk
authors.forename: Helen
authors.initials: H
authors.lastname: Walden
authors.forename: R Julio
authors.initials: RJ
authors.lastname: Martinez-Torres
mesh_terms: D006801:Humans; D008928:Mitochondria; D010300:Parkinson Disease / Q000378:metabolism*; D020734:Parkinsonian Disorders; D011494:Protein Kinases / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D044767:Ubiquitin-Protein Ligases / Q000235:genetics* / Q000378:metabolism*; D000099202:PTEN-Induced Putative Kinase
chemical_list: D011494:Protein Kinases; D044767:Ubiquitin-Protein Ligases; D000099202:PTEN-Induced Putative Kinase; C111567:parkin protein