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Published on: October 10, 2017
Metal Binding to Tau Protein: Physiological and Pathological Relevance.
Liliana Quintanar1,2, Gerardo U Juárez-Romero2, Gala R López-Herrera1
1Center for Research in Aging, Center for Research and Advanced Studies (Cinvestav), 14330 Mexico City, Mexico.
Biochemistry
|July 11, 2026
Summary
Metal ions like copper and zinc bind to tau protein, influencing its function and aggregation. This binding is crucial for understanding tauopathies such as Alzheimer's disease and metal homeostasis.
Area of Science:
- Bioinorganic Chemistry
- Neuroscience
- Protein Biochemistry
Background:
- Tau protein is intrinsically disordered, with diverse functions.
- Tau aggregation is a hallmark of tauopathies, including Alzheimer's disease.
- Metal ions (copper and zinc) interact with tau.
Purpose of the Study:
- Discuss recent advances in copper and zinc binding to tau.
- Explore the physiological and pathological relevance of metal-tau interactions.
- Examine the interplay between metal binding and tau's post-translational modifications (PTMs).
Main Methods:
- Literature review and perspective synthesis.
- Analysis of metal binding sites on tau.
- Discussion of tau's structural dynamics and aggregation.
Main Results:
- Metal binding sites on tau are located in regions involved in interactions with binding partners.
- Metal ions modulate tau's structural dynamics and amyloid aggregation.
- Metal ions may influence the diversity of tau fibril morphology.
- PTMs of tau can affect metal coordination, and metals can modulate PTM processing.
Conclusions:
- Metal binding plays a significant role in tau's interactome and functionality.
- Metal ions are potential drivers of tau's pathological transitions.
- Investigating metal ion roles in tau biology is crucial for understanding tauopathies and metal homeostasis.
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