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Updated: Jun 29, 2025
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Assay for Phosphorylation and Microtubule Binding Along with Localization of Tau Protein in Colorectal Cancer Cells
Published on: October 10, 2017
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Post-Translational Modifications Control Phase Transitions of Tau
Wyatt C Powell1, McKinley Nahum1, Karl Pankratz1
1Department of Chemistry, University of Colorado, Boulder, Colorado 80309, United States.
Biorxiv : the Preprint Server for Biology
|April 1, 2024
Summary
Post-translational modifications (PTMs) on Tau protein generally hinder the formation of paired helical filaments (PHFs) in Alzheimer's disease (AD) models. These modifications, especially phosphorylation, play a critical role in regulating Tau aggregation and liquid-liquid phase separation (LLPS).
Area of Science:
- Neuroscience
- Biochemistry
- Molecular Biology
Background:
- Tau protein self-assembles into paired helical filaments (PHFs) in Alzheimer's disease (AD) brains.
- The role of AD-specific post-translational modifications (PTMs) in PHF formation remains unclear.
- Understanding PTMs is crucial for elucidating Tau pathology in neurodegenerative diseases.
Conclusions:
- Site-specific PTMs and environmental factors intricately modulate Tau aggregation kinetics.
- PTMs, particularly those outside the ordered filament core, are critical regulators of Tau self-assembly into PHF structures.
- These findings enhance the understanding of molecular underpinnings of Tau pathology in Alzheimer's disease.
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