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Contribution of Alanine-76 and Serine Phosphorylation in alpha-Synuclein Membrane Association and Aggregation in Yeasts
Journal article   Open access   Peer reviewed

Contribution of Alanine-76 and Serine Phosphorylation in alpha-Synuclein Membrane Association and Aggregation in Yeasts

Michael Fiske, Stephanie Valtierra, Keith Solvang, Michael Zorniak, Michael White, Sara Herrera, Alina Konnikova, Rebecca Brezinsky and Shubhik DebBurman
Parkinson's disease, v 2011, p12
01 Jan 2011
PMID: 21826257
url
https://doi.org/10.4061/2011/392180View
Published, Version of Record (VoR) Open

Abstract

Clinical Neurology Life Sciences & Biomedicine Neurosciences & Neurology Science & Technology
In Parkinson's disease (PD), misfolded and aggregated alpha-synuclein protein accumulates in degenerating midbrain dopaminergic neurons. The amino acid alanine-76 in alpha-synuclein and phosphorylation at serine-87 and serine-129 are thought to regulate its aggregation and toxicity. However, their exact contributions to alpha-synuclein membrane association are less clear. We found that alpha-synuclein is indeed phosphorylated in fission yeast and budding yeast, the two models that we employed for assessing alpha-synuclein aggregation and membrane association properties, respectively. Surprisingly, blocking serine phosphorylation (S87A, S129A, and S87A/S129A) or mimicking it (S87D, S129D) altered alpha-synuclein aggregation in fission yeast. Either blocking or mimicking this phosphorylation increased endomembrane association in fission yeast, but only mimicking it decreased plasma membrane association in budding yeast. Polar substitution mutations of alanine-76 (A76E and A76R) decreased alpha-synuclein membrane association in budding yeast and decreased aggregation in fission yeast. These yeast studies extend our understanding of serine phosphorylation and alanine-76 contributions to alpha-synuclein aggregation and are the first to detail their impact on alpha-synuclein's plasma membrane and endomembrane association.

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