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April 30, 2026Journal of Biological ChemistryOpen Access

A coherent structural picture of the interaction of Tau with tubulin provides a link to its aggregation

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Authors

BGBenoı̂t GigantLKLiza Ammar KhodjaVCValérie Campanacci

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Overview

This research investigates Tau's interaction with tubulin, linking microtubule dynamics and aggregation in neurodegenerative diseases.

Key Points

  • To elucidate how Tau interacts with tubulin to influence microtubule assembly and aggregation mechanisms.
  • Integrated model of Tau-tubulin interactions based on various experimental approaches.
  • Analysis of Tau's binding mechanism to microtubules through specific and non-specific interactions.
  • Determination of a Tau:tubulin structural model to explore functional dynamics.
  • Characterization of Tau's modulating effects on microtubule dynamics through specific interactions along protofilaments and non-specific interactions with tubulin.
  • Establishment of a structural model showing a functional dimer of Tau interacting with microtubule apertures.
  • Discussion of potential connections between Tau dimerization and its oligomerization related to both healthy and pathological states.

Cite This Study

Gigant et al. (2026) studied this question.

synapsesocial.com/papers/69f2f0e31e5f7920c6386db9https://doi.org/10.1016/j.jbc.2026.113086
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