Abstract
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 parkins E3 ligase activity seems to play a pathogenic role in both inherited and sporadic Parkinsons disease (PD). Increasing evidence indicates that posttranslational modifications play a major role in regulating parkins 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.
Keywords: Dopamine, parkin, phosphorylation, S-nitrosylation, ubiquitylation, neurodegeneration, Parkinsonapos;s disease, signaling, substrate, protein interaction, localization
Current Medicinal Chemistry
Title: Posttranslational Modifications as Versatile Regulators of Parkin Function
Volume: 18 Issue: 16
Author(s): E. Rubio de la Torre, P. Gomez-Suaga, M. Martínez-Salvador and S. Hilfiker
Affiliation:
Keywords: Dopamine, parkin, phosphorylation, S-nitrosylation, ubiquitylation, neurodegeneration, Parkinsonapos;s disease, signaling, substrate, protein interaction, localization
Abstract: 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 parkins E3 ligase activity seems to play a pathogenic role in both inherited and sporadic Parkinsons disease (PD). Increasing evidence indicates that posttranslational modifications play a major role in regulating parkins 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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Cite this article as:
Rubio de la Torre E., Gomez-Suaga P., Martínez-Salvador M. and Hilfiker S., Posttranslational Modifications as Versatile Regulators of Parkin Function, Current Medicinal Chemistry 2011; 18 (16) . https://dx.doi.org/10.2174/092986711795843254
DOI https://dx.doi.org/10.2174/092986711795843254 |
Print ISSN 0929-8673 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-533X |
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