ArticleBiophysical journal2017
Heterogeneous Tau-Tubulin Complexes Accelerate Microtubule Polymerization.
Article in Biophysical journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 40 citations in OpenAlex.
- N-Terminal Amine Chemistry Influences α-Synuclein Interactions with Lipid Bilayers.Biochemistry · 2026Article
- FGF-Mediated Axon Guidance: Role of Downstream Signaling Pathways in Cytoskeletal Control.Cells · 2025Review
- Structural insights into the role of the proline rich region in tau function.Structure (London, England : 1993) · 2025Article
- Mixtures of Intrinsically Disordered Neuronal Protein Tau and Anionic Liposomes Reveal Distinct Anionic Liposome-Tau Complexes Coexisting with Tau Liquid-Liquid Phase Separated Coacervates.bioRxiv : the preprint server for biology · 2024Article
- Complexes of tubulin oligomers and tau form a viscoelastic intervening network cross-bridging microtubules into bundles.Nature communications · 2024Article
- Article
- Combining non-canonical amino acid mutagenesis and native chemical ligation for multiply modifying proteins: A case study of α-synuclein post-translational modifications.Methods (San Diego, Calif.) · 2023Article
- Microtubule-binding core of the tau protein.Science advances · 2022Article
- Dichotomous role of microtubule associated protein tau as a biomarker of response to and a target for increasing efficacy of taxane treatment in cancers of epithelial origin.Pharmacological research · 2021Review
- Structural Characterization of Tau in Fuzzy Tau:Tubulin Complexes.Structure (London, England : 1993) · 2020Article
- Acute inhibition of the CNS-specific kinase TTBK1 significantly lowers tau phosphorylation at several disease relevant sites.PloS one · 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
- Polyphosphate Initiates Tau Aggregation through Intra- and Intermolecular Scaffolding.Biophysical journal · 2019Article
- Tau isoform-specific stabilization of intermediate states during microtubule assembly and disassembly.The Journal of biological chemistry · 2019Article
- Identification of N-linked glycans as specific mediators of neuronal uptake of acetylated α-Synuclein.PLoS biology · 2019Article
- Untangling the Conformational Polymorphism of Disordered Proteins Associated With Neurodegeneration at the Single-Molecule Level.Frontiers in molecular neuroscience · 2019Review
- Visualization of Tau⁻Tubulin Interaction in a Living Cell Using Bifluorescence Complementation Technique.International journal of molecular sciences · 2018Article
- IDPs in macromolecular complexes: the roles of multivalent interactions in diverse assemblies.Current opinion in structural biology · 2018Review
- Imbalanced Expression of Tau and Tubulin Induces Neuronal Dysfunction inFrontiers in neuroscience · 2018Article
- Local Nucleation of Microtubule Bundles through Tubulin Concentration into a Condensed Tau Phase.Cell reports · 2017Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
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Abstract
Tau is an intrinsically disordered protein with a central role in the pathology of a number of neurodegenerative diseases. Tau normally functions to stabilize neuronal microtubules, although the mechanism underlying this function is not well understood. Of note is that the interaction between tau and soluble tubulin, which has implications both in understanding tau function as well as its role in disease, is underexplored. Here we investigate the relationship between heterogeneity in tau-tubulin complexes and tau function. Specifically, we created a series of truncated and scrambled tau constructs and characterized the size and heterogeneity of the tau-tubulin complexes formed under nonpolymerizing conditions. Function of the constructs was verified by tubulin polymerization assays. We find that, surprisingly, the pseudo-repeat region of tau, which flanks the core microtubule-binding domain of tau, contributes largely to the formation of large, heterogeneous tau tubulin complexes; additional independent tubulin binding sites exist in repeats two and three of the microtubule binding domain. Of particular interest is that we find positive correlation between the size and heterogeneity of the complexes and rate of tau-promoted microtubule polymerization. We propose that tau-tubulin can be described as a "fuzzy" complex, and our results demonstrate the importance of heterogeneous complex formation in tau function. This work provides fundamental insights into the functional mechanism of tau, and more broadly underscores the relevance of heterogeneous and dynamic complexes in the functions of intrinsically disordered proteins.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.