ArticleThe Journal of biological chemistry2011
The C terminus of tubulin, a versatile partner for cationic molecules: binding of Tau, polyamines, and calcium.
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 26 papers.
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Who cites it
26 citing papers in PubMed, 55 citations in OpenAlex.
- A coherent structural picture of the interaction of Tau with tubulin provides a link to its aggregation.The Journal of biological chemistry · 2026Review
- Article
- Tau protein in Parkinson's disease: advances in phosphoproteomics and molecular dynamics simulations.Frontiers in aging neuroscience · 2026Review
- Modulation of microtubule dynamics by monovalent ions.PNAS nexus · 2025Article
- Myotoxin-3 from the Pacific RattlesnakeMolecules (Basel, Switzerland) · 2022Article
- Genome-Wide Identification and Characterization of RNA/DNA Differences Associated withInternational journal of molecular sciences · 2022Article
- Aberrant AZIN2 and polyamine metabolism precipitates tau neuropathology.The Journal of clinical investigation · 2021Article
- Mutations disrupting neuritogenesis genes confer risk for cerebral palsy.Nature genetics · 2020Article
- A Simple and Scalable Strategy for Analysis of Endogenous Protein Dynamics.Scientific reports · 2020Article
- Structural Characterization of Tau in Fuzzy Tau:Tubulin Complexes.Structure (London, England : 1993) · 2020Article
- The disordered N-terminus of HDAC6 is a microtubule-binding domain critical for efficient tubulin deacetylation.The Journal of biological chemistry · 2020Article
- Direct observation of dynamic protein interactions involving human microtubules using solid-state NMR spectroscopy.Nature communications · 2020Article
- Tubulin response to intense nanosecond-scale electric field in molecular dynamics simulation.Scientific reports · 2019Article
- Regulation of microtubule dynamic instability by the carboxy-terminal tail of β-tubulin.Life science alliance · 2018Article
- Calcium-axonemal microtubuli interactions underlie mechanism(s) of primary cilia morphological changes.Journal of biological physics · 2018Article
- Imbalanced Expression of Tau and Tubulin Induces Neuronal Dysfunction inFrontiers in neuroscience · 2018Article
- An Emerging Role for Tubulin Isotypes in Modulating Cancer Biology and Chemotherapy Resistance.International journal of molecular sciences · 2017Review
- Polarity of varicosity initiation in central neuron mechanosensation.The Journal of cell biology · 2017Article
- Heterogeneous Tau-Tubulin Complexes Accelerate Microtubule Polymerization.Biophysical journal · 2017Article
- Sustained Arginase 1 Expression Modulates Pathological Tau Deposits in a Mouse Model of Tauopathy.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2015Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The C-terminal region of tubulin is involved in multiple aspects of the regulation of microtubule assembly. To elucidate the molecular mechanisms of this regulation, we study here, using different approaches, the interaction of Tau, spermine, and calcium, three representative partners of the tubulin C-terminal region, with a peptide composed of the last 42 residues of α1a-tubulin. The results show that their binding involves overlapping amino acid stretches in the C-terminal tubulin region: amino acid residues 421-441 for Tau, 430-432 and 444-451 for spermine, and 421-443 for calcium. Isothermal titration calorimetry, NMR, and cosedimentation experiments show that Tau and spermine have similar micromolar binding affinities, whereas their binding stoichiometry differs (C-terminal tubulin peptide/spermine stoichiometry 1:2, and C-terminal tubulin peptide/Tau stoichiometry 8:1). Interestingly, calcium, known as a negative regulator of microtubule assembly, can compete with the binding of Tau and spermine with the C-terminal domain of tubulin and with the positive effect of these two partners on microtubule assembly in vitro. This observation opens up the possibility that calcium may participate in the regulation of microtubule assembly in vivo through direct (still unknown) or indirect mechanism (displacement of microtubule partners). The functional importance of this part of tubulin was also underlined by the observation that an α-tubulin mutant deleted from the last 23 amino acid residues does not incorporate properly into the microtubule network of HeLa cells. Together, these results provide a structural basis for a better understanding of the complex interactions and putative competition of tubulin cationic partners with the C-terminal region of tubulin.
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