Liquid–liquid phase separation of tau protein: The crucial role of electrostatic interactions
| Autor: | Solomiia Boyko, Krystyna Surewicz, Witold K. Surewicz, Tien-Hao Chen, Xu Qi |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: |
0301 basic medicine
Tau protein Static Electricity Context (language use) tau Proteins neurodegeneration protein aggregation Biochemistry Protein Aggregation Pathological Protein–protein interaction Hydrophobic effect protein-protein interaction 03 medical and health sciences neurodegenerative disease medicine Humans Editors' Picks protein misfolding Phosphorylation Molecular Biology 030102 biochemistry & molecular biology biology Mechanism (biology) Chemistry tauopathy Cell Biology Alzheimer's disease medicine.disease intrinsically disordered protein 030104 developmental biology liquid-liquid phase separation (LLPS) Biophysics biology.protein Protein folding Tauopathy Tau protein (Tau) Hydrophobic and Hydrophilic Interactions |
| Zdroj: | The Journal of Biological Chemistry Journal of Biological Chemistry |
| ISSN: | 1083-351X 0021-9258 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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