May 18, 2019

Liquid-liquid phase separation of tau protein: The crucial role of electrostatic interactions

The Journal of Biological Chemistry
Solomiia BoykoWitold K Surewicz

Abstract

Recent studies have indicated that tau, a protein involved in Alzheimer's disease and other neurodegenerative disorders, has a propensity to undergo liquid-liquid phase separation (LLPS). However, the mechanism of this process remains unknown. Here, we demonstrate that tau LLPS is largely driven by intermolecular electrostatic interactions between the negatively charged N-terminal and positively charged middle/C-terminal regions, whereas hydrophobic interactions play a surprisingly small role. Furthermore, our results reveal that, in contrast to previous suggestions, phosphorylation is not required for tau LLPS. These findings provide a foundation for understanding the mechanism by which phosphorylation and other posttranslational modifications could modulate tau LLPS in the context of specific physiological functions as well as pathological interactions.

  • References31
  • Citations6

References

  • References31
  • Citations6

Citations

Mentioned in this Paper

Study
Post-Translational Protein Processing
Ions
Alzheimer's Disease
Tau Proteins
Neurodegenerative Disorders
Liquid-Liquid Extraction
Liquid Diet
Phosphorylation

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