Phosphorylation modifies the molecular stability of β-amyloid deposits

Nasrollah Rezaei-Ghaleh (), Mehriar Amininasab, Sathish Kumar, Jochen Walter () and Markus Zweckstetter ()
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Nasrollah Rezaei-Ghaleh: German Center for Neurodegenerative Diseases (DZNE)
Mehriar Amininasab: School of Biology, College of Science, University of Tehran
Sathish Kumar: University of Bonn
Jochen Walter: University of Bonn
Markus Zweckstetter: German Center for Neurodegenerative Diseases (DZNE)

Nature Communications, 2016, vol. 7, issue 1, 1-9

Abstract: Abstract Protein aggregation plays a crucial role in neurodegenerative diseases. A key feature of protein aggregates is their ubiquitous modification by phosphorylation. Little is known, however, about the molecular consequences of phosphorylation of protein aggregates. Here we show that phosphorylation of β-amyloid at serine 8 increases the stability of its pathogenic aggregates against high-pressure and SDS-induced dissociation. We further demonstrate that phosphorylation results in an elevated number of hydrogen bonds at the N terminus of β-amyloid, the region that is critically regulated by a variety of post-translational modifications. Because of the increased lifetime of phosphorylated β-amyloid aggregates, phosphorylation can promote the spreading of β-amyloid in Alzheimer pathogenesis. Our study suggests that regulation of the molecular stability of protein aggregates by post-translational modifications is a crucial factor for disease progression in the brain.

Date: 2016
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DOI: 10.1038/ncomms11359

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