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Grenoble Institut des Neurosciences Grenoble Institut des Neurosciences

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Truncation of tau and cytoskeleton alteration

Objectifs

Truncated forms of tau are present in neurons during brain disorders like Alzheimer’s disease. These truncated proteins may exhibit toxic gain of functions, leading to cytoskeleton changes and neuronal impairments. The main objective is to investigate how tau fragments affect cytoskeleton properties.

Résumé

Tau is a cytoskeleton-associated protein involved in microtubule and actin regulation, which contributes to the proper functions of neurons. Since the identification of tau as a major component of the neurofibrillary tangles characterizing Alzheimer’s disease, much attention has been given to tau aggregative properties. However, recent studies have proposed that soluble truncated forms of tau exhibit toxic gain of functions, leading to cytoskeleton changes and neuronal impairments. Yet, the mechanisms by which these truncated forms alter microtubule and actin networks are still unknown. The student will explore the cytoskeleton-regulative properties of tau fragments in cells by using a system based on TEV protease. This system allows time- and site-specific control of tau cleavage, and all the tools necessary for its use are already available in the laboratory. This original approach will be first applied to fibroblasts, which represent a well-characterized model to study microtubule and actin behaviour, and then to primary cultured neurons.

Méthodes

Cell culture (primary fibroblasts and neurons), transfection, transduction with lentiviral vectors, immunofluorescence, confocal microscopy, live-cell imaging and molecular biology.

Références

  • Ramirez-Rios, S., E. Denarier, A. Vinit, E. Prezel, V. Stoppin-Mellet, L. Peris, A. Andrieux, L. Serre, A. Fourest-Lieuvin, and I. Arnal. 2016. Tau antagonizes EB tracking at microtubule ends through a phosphorylation-dependent mechanism. Mol biol cell. 27:2924-34.
  • Osseni, A., M. Sébastien, O. Sarrault, M. Baudet, Y. Couté, J. Fauré, A. Fourest-Lieuvin*, and I. Marty*. 2016. Triadin and CLIMP-63 form a link betwen triads and microtubules in muscle cells. J Cell Sci. 129:3744-55.*co-senior
  • Elie, A., E. Prezel, C. Guerin, E. Denarier, S. Ramirez-Rios, L. Serre, A. Andrieux, A. Fourest-Lieuvin, L. Blanchoin, and I. Arnal. 2015. Tau co-organizes dynamic microtubule and actin networks. Scientific reports. 5:9964.

Contacts

Anne Fourest-Lieuvin, Chercheur CEA
Email : anne.fourest-lieuvin@univ-grenoble-alpes.fr

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Mise à jour le 23 mai 2017

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