Titre :

Two Tau binding sites on tubulin revealed by thiol-disulfide exchanges

Auteur(s) :

Martinho, Marlène [Auteur]
Aix Marseille Université [AMU]
Allegro, Diane [Auteur]
Aix Marseille Université [AMU]
Huvent, Isabelle [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Chabaud, Charlotte [Auteur]
Aix Marseille Université [AMU]
Etienne, Emilien [Auteur]
Aix Marseille Université [AMU]
Kovacic, Hervé [Auteur]
Aix Marseille Université [AMU]
Guigliarelli, Bruno [Auteur]
Aix Marseille Université [AMU]
Peyrot, Vincent [Auteur]
Aix Marseille Université [AMU]
Landrieu, Isabelle [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Belle, Valérie [Auteur]
Aix Marseille Université [AMU]
Barbier, Pascale [Auteur]
Aix Marseille Université [AMU]

Titre de la revue :

Scientific Reports

Numéro :

8

Pagination :

13846

Date de publication :

2018-09-14

ISSN :

2045-2322

Discipline(s) HAL :

Chimie/Chimie théorique et/ou physique

Résumé en anglais : [en]

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 ...
Lire la suite >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.Lire moins >

Langue :

Anglais

Audience :

Internationale

Vulgarisation :

Non

Établissement(s) :

CNRS
Université de Lille

Collections :

• Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576

Équipe(s) de recherche :

Chemical Glycobiology

Date de dépôt :

2020-02-12T15:45:31Z
2024-02-19T12:49:32Z