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Grenoble Institut des Neurosciences Grenoble Institut des Neurosciences

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Interaction of tau and microtubules using single molecule approach

Objectifs

By characterizing the dynamic interaction of physiological tau protein and pathological tau mutants with microtubules, we aim to understand how tau dysfunctions lead to cytoskeletal alterations.

Résumé

Tau is a neuronal Microtubule-Associated Protein that regulates microtubule (MT) assembly and organization in axons. Misregulation of tau leads to cytoskeleton alterations and severe neuronal impairment in several neurodegenerative pathologies like Alzheimer’s Disease and related dementia. Although it is known for years that tau forms aggregates in the late stages of the disease, we still lack a clear picture of how soluble forms of tau interacts with the cytoskeleton in the earlier stages.
To address this issue, we developed biomimetic assays that reconstitute MT arrays as observed in cells. Using high resolution TIRF microscopy, we can observe in real time single molecules of tau that interact with dynamic MT. This approach allows us to characterize the complex dynamic interaction of tau with MT. We will compare the behavior of normal tau with mutated forms of tau found in the brains of Alzheimer’s patients.

Méthodes

Total Internal Reflection Fluorescence Microscopy (TIRFM) – Protein purification – Molecular cloning – Image analysis (Image J software).

Références

  • Ramirez-Rios S, Denarier E, Prezel E, Vinit A, Stoppin-Mellet V, Devred F, Barbier P, Peyrot V, Sayas CL, Avila J, Peris L, Andrieux A, Serre L, Fourest-Lieuvin A and Arnal I. (2016) Tau antagonizes EB tracking at microtubule ends through a phosphorylation-dependent mechanism. Mol Biol Cell, 27:2924-34.

  • Elie A, Prezel E, Guérin C, Denarier E, Ramirez-Rios S, Serre L, Andrieux A, Fourest-Lieuvin A, Blanchoin L and Arnal I (2015) Tau co-organizes dynamic microtubule and actin networks. Sci Rep 5:9964.

  • Sayas CL, Tortosa E, Bollati F, Ramirez-Rios S, Arnal I and Avila J (2015) Tau regulates the localization and function of End binding proteins 1 and 3 (EB1/3) in neuronal cells. J. Neurochem, 133, 653-667.

Contacts

Virginie Stoppin-Mellet, MCF UGA
Email : virginie.stoppin-mellet@univ-grenoble-alpes.fr


Mise à jour le 7 juin 2017

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