Journal
CURRENT MEDICINAL CHEMISTRY
Volume 18, Issue 16, Pages 2477-2485Publisher
BENTHAM SCIENCE PUBL LTD
DOI: 10.2174/092986711795843254
Keywords
Dopamine; parkin; phosphorylation; S-nitrosylation; ubiquitylation; neurodegeneration; Parkinson's disease; signaling; substrate; protein interaction; localization
Funding
- Spanish Ministry of Science and Innovation (MICINN) [SAF2009-11292, 200920I126]
- Spanish Ministry of Health (FIS) [PI080010]
- Spanish Federation of Parkinson's Disease (FEP)
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Parkin functions as an E3 ubiquitin ligase that monoubiquitylates and polyubiquitylates proteins to regulate a variety of cellular processes. It appears that parkin functions as a multipurpose neuroprotectant in a number of toxic paradigms, and loss of parkin's E3 ligase activity seems to play a pathogenic role in both inherited and sporadic Parkinson's disease (PD). Increasing evidence indicates that posttranslational modifications play a major role in regulating parkin's catalytic activity, solubility, substrate selection or subcellular localization. As some of these modification events are subject to pharmacological interventions, these findings may allow for new approaches in preventing or delaying PD onset and/or progression. Here, we review how posttranslational modifications can regulate this unique multifaceted ubiquitin ligase which plays a crucial role for the survival of dopaminergic neurons.
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