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Updated: Jun 20, 2026

Assay for Phosphorylation and Microtubule Binding Along with Localization of Tau Protein in Colorectal Cancer Cells
Published on: October 10, 2017
Post-translational modifications as a regulatory code for tau function in health and disease
Abigail J Nordbeck1,2, Bhirisha Sharma1,2, Charles A Garcia1
1Arizona State University-Banner Neurodegenerative Disease Research Center at the Biodesign Institute, Tempe, AZ, United States.
Tau protein modifications (PTMs) normally regulate neuronal function but become disrupted in tauopathies. Understanding these PTM networks is key to developing therapies for neurodegenerative diseases like Alzheimer's.
Area of Science:
- Neuroscience
- Molecular Biology
- Biochemistry
Background:
- Tau is a microtubule-associated protein crucial for neuronal function.
- Post-translational modifications (PTMs) dynamically regulate tau's structure and function.
- Disrupted PTMs in tauopathies lead to toxic tau aggregation and neurodegeneration.
Purpose of the Study:
- To review the diverse PTMs of tau protein.
- To explore the integrated network of tau PTMs and their crosstalk.
- To discuss the role of PTM dysregulation in neurodegenerative diseases.
Main Methods:
- Literature review of tau PTMs.
- Analysis of proteomic studies on tau modifications.
- Synthesis of current knowledge on PTM interactions and dysregulation.
Main Results:
- Tau undergoes numerous PTMs (acetylation, ubiquitination, etc.) beyond phosphorylation.
- PTMs function as an integrated network, with crosstalk influencing tau's pathogenic potential.
- Dysregulated PTM networks contribute to tau aggregation and neurodegeneration.
Conclusions:
- Understanding tau PTM networks is essential for comprehending tauopathies.
- Targeting enzymes that regulate tau PTMs offers potential therapeutic strategies for Alzheimer's disease and related disorders.
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