期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 294, 期 29, 页码 11054-11059出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.AC119.009198
关键词
Tau protein (Tau); protein misfolding; tauopathy; neurodegenerative disease; protein-protein interaction; intrinsically disordered protein; liquid-liquid phase separation (LLPS); Alzheimer's disease; neurodegeneration; protein aggregation
资金
- National Institutes of Health [RF1 AG061797]
- Department of Physiology and Biophysics, Case Western Reserve University
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.
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