ArticleMolecular biology of the cell2018
Tau can switch microtubule network organizations: from random networks to dynamic and stable bundles.
Article in Molecular biology of the cell, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed.
- A coherent structural picture of the interaction of Tau with tubulin provides a link to its aggregation.The Journal of biological chemistry · 2026Review
- Drosophila wing is a high-throughput and versatile screening tool for Tau-mediated disease mechanisms and drug discovery.Disease models & mechanisms · 2026Article
- SSNA1 mechanically reinforces the damaged microtubule lattice.bioRxiv : the preprint server for biology · 2026Article
- Article
- Tau-Targeted Therapeutic Strategies: Mechanistic Targets, Clinical Pipelines, and Analysis of Failures.Cells · 2025Review
- The N-terminal domain of COMPANION OF CELLULOSE SYNTHASE1 promotes microtubule array formation in Arabidopsis.Plant physiology · 2025Article
- Are Hippocampal Hypoperfusion and ATP Depletion Prime Movers in the Genesis of Alzheimer's Disease? A Review of Recent Pertinent Observations from Molecular Biology.International journal of molecular sciences · 2025Review
- Loss of Eml1 alters microtubule-associated protein networks in mouse brain heterotopia.Communications biology · 2025Article
- Tau-seed interactome analysis reveals distinct functional signatures in Alzheimer's disease across model systems.bioRxiv : the preprint server for biology · 2025Article
- Hydrolysis-deficient mosaic microtubules as faithful mimics of the GTP cap.Nature communications · 2025Article
- Flavonoids and Alzheimer's disease: reviewing the evidence for neuroprotective potential.Molecular and cellular biochemistry · 2025Review
- The structure of a Tau fragment bound to tubulin prompts new hypotheses on Tau mechanism and oligomerization.PNAS nexus · 2024Article
- The multiple roles of chronic stress and glucocorticoids in Alzheimer's disease pathogenesis.Trends in neurosciences · 2024Review
- Article
- Comprehensive Insights into Pathophysiology of Alzheimer's Disease: Herbal Approaches for Mitigating Neurodegeneration.Current Alzheimer research · 2024Review
- A Network of 17 Microtubule-Related Genes Highlights Functional Deregulations in Breast Cancer.Cancers · 2023Article
- Microtubules composed of α4A undergo curved growth mainly mediated by its core structure.Journal of molecular cell biology · 2023Article
- Advances in Understanding the Molecular Mechanisms of Neuronal Polarity.Molecular neurobiology · 2023Review
- All the Tau We Cannot See.Annual review of medicine · 2023Review
- Multiple pathways promote microtubule stabilization in senescent intestinal epithelial cells.npj aging · 2022Article
Corrections and comments
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In neurons, microtubule networks alternate between single filaments and bundled arrays under the influence of effectors controlling their dynamics and organization. Tau is a microtubule bundler that stabilizes microtubules by stimulating growth and inhibiting shrinkage. The mechanisms by which tau organizes microtubule networks remain poorly understood. Here, we studied the self-organization of microtubules growing in the presence of tau isoforms and mutants. The results show that tau's ability to induce stable microtubule bundles requires two hexapeptides located in its microtubule-binding domain and is modulated by its projection domain. Site-specific pseudophosphorylation of tau promotes distinct microtubule organizations: stable single microtubules, stable bundles, or dynamic bundles. Disease-related tau mutations increase the formation of highly dynamic bundles. Finally, cryo-electron microscopy experiments indicate that tau and its variants similarly change the microtubule lattice structure by increasing both the protofilament number and lattice defects. Overall, our results uncover novel phosphodependent mechanisms governing tau's ability to trigger microtubule organization and reveal that disease-related modifications of tau promote specific microtubule organizations that may have a deleterious impact during neurodegeneration.
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