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Tau interaction with microtubules in vivo
Andrey Samsonov1, Jiang-Zhou Yu, Mark Rasenick
1Department of Physiology and Biophysics M/C 901, University of Illinois at Chicago, 835 S. Wolcott Avenue, Chicago, IL 60612, USA.
Journal of Cell Science
|November 27, 2004
Summary
Tau protein dynamically interacts with microtubules (MTs) in neurons. This interaction influences MT stability and shape, suggesting a role in neuronal plasticity and cytoskeleton remodeling.
Area of Science:
- Neuroscience
- Cell Biology
- Biochemistry
Background:
- Tau is a key microtubule-associated protein (MAP) crucial for axonal microtubule (MT) bundling and stabilization.
- Understanding tau's dynamic interaction with MTs in living neurons is essential for elucidating neuronal cytoskeleton regulation.
Purpose of the Study:
- To investigate the dynamic interaction of tau with microtubules (MTs) in living neuronal cells.
- To explore how tau binding to MTs is affected by MT dynamics and structure.
Main Methods:
- Expression of GFP-tau fusion protein in cultured Xenopus embryo neurons.
- Time-lapse imaging of tau-labeled MTs.
- Photobleaching experiments to assess tau-MT interaction dynamics.
- Treatment with taxol to alter MT dynamics.
Main Results:
- Tau uniformly labeled individual MTs irrespective of their assembly status or axonal location.
- Tau-MT interactions are highly dynamic, with a fluorescence recovery half-time of approximately 3 seconds.
- Taxol-induced suppression of MT dynamics led to rapid tau detachment.
- Tau showed uniform binding to straight MTs but concentrated at sites of high MT curvature.
Conclusions:
- The dynamic interaction of tau with MTs suggests a role in modulating local MT mechanical properties.
- Tau's preferential binding at MT curvatures may be critical for MT cytoskeleton remodeling during neuronal plasticity.