ArticleScientific reports2018
Two Tau binding sites on tubulin revealed by thiol-disulfide exchanges.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 30 citations in OpenAlex.
- Metal Binding to Tau Protein: Physiological and Pathological Relevance.Biochemistry · 2026Review
- A coherent structural picture of the interaction of Tau with tubulin provides a link to its aggregation.The Journal of biological chemistry · 2026Review
- Nitroxide spin, non-canonical amino acids and SDSL-EPR spectroscopy: a winning combination for protein dynamics studies.European biophysics journal : EBJ · 2026Article
- Hidden protein disorder: Deciphering the structural organisation and dynamics of a non-canonical CP12 from the diatom Thalassiosira pseudonana.The FEBS journal · 2025Article
- Structural insights into the role of the proline rich region in tau function.Structure (London, England : 1993) · 2025Article
- Cellular Uptake of Tau Aggregates Triggers Disulfide Bond Formation in Four-Repeat Tau Monomers.ACS chemical neuroscience · 2025Article
- Structural Flexibility of Tau in Its Interaction with Microtubules as Viewed by Site-Directed Spin Labeling EPR Spectroscopy.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Role of the Cysteine in R3 Tau Peptide in Copper Binding and Reactivity.International journal of molecular sciences · 2022Article
- Mical modulates Tau toxicity via cysteine oxidation in vivo.Acta neuropathologica communications · 2022Article
- Disulfide bond formation in microtubule-associated tau protein promotes tau accumulation and toxicity in vivo.Human molecular genetics · 2021Article
- The Two Cysteines of Tau Protein Are Functionally Distinct and Contribute Differentially to Its PathogenicityThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2021Article
- Extensive Anti-CoA Immunostaining in Alzheimer's Disease and Covalent Modification of Tau by a Key Cellular Metabolite Coenzyme A.Frontiers in cellular neuroscience · 2021Article
- Structural Characterization of Tau in Fuzzy Tau:Tubulin Complexes.Structure (London, England : 1993) · 2020Article
- The mechanism of Hsp90-induced oligomerizaton of Tau.Science advances · 2020Article
- Tau isoform-specific stabilization of intermediate states during microtubule assembly and disassembly.The Journal of biological chemistry · 2019Article
- Tau repeat regions contain conserved histidine residues that modulate microtubule-binding in response to changes in pH.The Journal of biological chemistry · 2019Article
- The elusive tau molecular structures: can we translate the recent breakthroughs into new targets for intervention?Acta neuropathologica communications · 2019Review
- Role of Tau as a Microtubule-Associated Protein: Structural and Functional Aspects.Frontiers in aging neuroscience · 2019Article
Corrections and comments
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Authors and funding
11 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tau is a Microtubule-associated protein that induces and stabilizes the formation of the Microtubule cytoskeleton and plays an important role in neurodegenerative diseases. The Microtubules binding region of Tau has been determined for a long time but where and how Tau binds to its partner still remain a topic of debate. We used Site Directed Spin Labeling combined with EPR spectroscopy to monitor Tau upon binding to either Taxol-stabilized MTs or to αβ-tubulin when Tau is directly used as an inducer of MTs formation. Using maleimide-functionalized labels grafted on the two natural cysteine residues of Tau, we found in both cases that Tau remains highly flexible in these regions confirming the fuzziness of Tau:MTs complexes. More interestingly, using labels linked by a disulfide bridge, we evidenced for the first time thiol disulfide exchanges between αβ-tubulin or MTs and Tau. Additionally, Tau fragments having the two natural cysteines or variants containing only one of them were used to determine the role of each cysteine individually. The difference observed in the label release kinetics between preformed MTs or Tau-induced MTs, associated to a comparison of structural data, led us to propose two putative binding sites of Tau on αβ-tubulin.
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Registered trials
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.