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Phosphorylation modifies the molecular stability of β-amyloid deposits

Author

Listed:
  • 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)
    Max Planck Institute for Biophysical Chemistry
    University Medical Center Göttingen, University of Göttingen)

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.

Suggested Citation

  • Nasrollah Rezaei-Ghaleh & Mehriar Amininasab & Sathish Kumar & Jochen Walter & Markus Zweckstetter, 2016. "Phosphorylation modifies the molecular stability of β-amyloid deposits," Nature Communications, Nature, vol. 7(1), pages 1-9, September.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms11359
    DOI: 10.1038/ncomms11359
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