ArticleThe Journal of biological chemistry2011
Systematic identification of tubulin-interacting fragments of the microtubule-associated protein Tau leads to a highly efficient promoter of microtubule assembly.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed.
- Janus Polymeric Nanorods Inhibit human Amylin Oligomerization and Fibrillation for Potential Type 2 Diabetes Treatment.Small science · 2026Article
- A coherent structural picture of the interaction of Tau with tubulin provides a link to its aggregation.The Journal of biological chemistry · 2026Review
- Tau protein in Parkinson's disease: advances in phosphoproteomics and molecular dynamics simulations.Frontiers in aging neuroscience · 2026Review
- The structure of a Tau fragment bound to tubulin prompts new hypotheses on Tau mechanism and oligomerization.PNAS nexus · 2024Article
- Nanotechnology for tau pathology in Alzheimer's disease.Materials today. Bio · 2024Review
- Membrane-induced tau amyloid fibrils.Communications biology · 2023Article
- Recent Advances in the Molecular and Cellular Mechanisms of gp120-Mediated Neurotoxicity.Cells · 2022Review
- Tau forms oligomeric complexes on microtubules that are distinct from tau aggregates.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- TANGLED1 mediates microtubule interactions that may promote division plane positioning in maize.The Journal of cell biology · 2020Article
- Structural Characterization of Tau in Fuzzy Tau:Tubulin Complexes.Structure (London, England : 1993) · 2020Article
- Human Dental Pulp Stem Cells Display a Potential for Modeling Alzheimer Disease-Related Tau Modifications.Frontiers in neurology · 2020Article
- Independent tubulin binding and polymerization by the proline-rich region of Tau is regulated by Tau's N-terminal domain.The Journal of biological chemistry · 2019Article
- Dynamical decoration of stabilized-microtubules by Tau-proteins.Scientific reports · 2019Article
- The complexity of tau in Alzheimer's disease.Neuroscience letters · 2019Review
- Major Differences between the Self-Assembly and Seeding Behavior of Heparin-Induced and in Vitro Phosphorylated Tau and Their Modulation by Potential Inhibitors.ACS chemical biology · 2019Article
- Elucidating Tau function and dysfunction in the era of cryo-EM.The Journal of biological chemistry · 2019Review
- The companion of cellulose synthase 1 confers salt tolerance through a Tau-like mechanism in plants.Nature communications · 2019Article
- Role of Tau as a Microtubule-Associated Protein: Structural and Functional Aspects.Frontiers in aging neuroscience · 2019Article
- Two Tau binding sites on tubulin revealed by thiol-disulfide exchanges.Scientific reports · 2018Article
- Therapeutic Strategies for Restoring Tau Homeostasis.Cold Spring Harbor perspectives in medicine · 2018Review
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tau is a microtubule-associated protein that stabilizes microtubules and stimulates their assembly. Current descriptions of the tubulin-interacting regions of Tau involve microtubules as the target and result mainly from deletions of Tau domains based on sequence analysis and from NMR spectroscopy experiments. Here, instead of microtubules, we use the complex of two tubulin heterodimers with the stathmin-like domain of the RB3 protein (T(2)R) to identify interacting Tau fragments generated by limited proteolysis. We show that fragments in the proline-rich region and in the microtubule-binding repeats domain each interact on their own not only with T(2)R but also with microtubules, albeit with moderate affinity. NMR analysis of the interaction with T(2)R of constructs in these two regions leads to a fragment, composed of adjacent parts of the microtubule-binding repeat domain and of the proline-rich region, that binds tightly to stabilized microtubules. This demonstrates the synergy of the two Tau regions we identified in the Tau-microtubule interaction. Moreover, we show that this fragment, which binds to two tubulin heterodimers, stimulates efficiently microtubule assembly.
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