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Proteasomal Inhibition as a Treatment Strategy for Parkinson's Disease: The Impact of α-Synuclein on Nurr1

Michael J. Devine
Journal of Neuroscience 14 November 2012, 32 (46) 16071-16073; DOI: https://doi.org/10.1523/JNEUROSCI.4224-12.2012
Michael J. Devine
Department of Molecular Neuroscience, Institute of Neurology, University College London, London WC1N 3BG, United Kingdom
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    Figure 1.

    The relationship between Nurr1 and α-synuclein under different proteasomal conditions. A, Under steady-state conditions, each protein negatively regulates the abundance of the other. Nurr1 inhibits the transcription of α-synuclein, while α-synuclein expedites the proteasomal breakdown of Nurr1. B, With brief, partial proteasomal inhibition, α-synuclein loses its ability to negatively regulate Nurr1, but Nurr1 can still inhibit α-synuclein. A positive feedback loop is created, favoring Nurr1. C, With chronic, complete proteasomal inhibition, existing models predict that α-synuclein will accumulate, despite Nurr1 being relieved of negative regulation. This suggests that Nurr1 levels can be suppressed by other means or that Nurr1 activity is impaired after α-synuclein levels become too high.

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The Journal of Neuroscience: 32 (46)
Journal of Neuroscience
Vol. 32, Issue 46
14 Nov 2012
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Proteasomal Inhibition as a Treatment Strategy for Parkinson's Disease: The Impact of α-Synuclein on Nurr1
Michael J. Devine
Journal of Neuroscience 14 November 2012, 32 (46) 16071-16073; DOI: 10.1523/JNEUROSCI.4224-12.2012

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Proteasomal Inhibition as a Treatment Strategy for Parkinson's Disease: The Impact of α-Synuclein on Nurr1
Michael J. Devine
Journal of Neuroscience 14 November 2012, 32 (46) 16071-16073; DOI: 10.1523/JNEUROSCI.4224-12.2012
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