Mechanism of Tau-Promoted Microtubule ...
Document type :
Article dans une revue scientifique
DOI :
Permalink :
Title :
Mechanism of Tau-Promoted Microtubule Assembly As Probed by NMR Spectroscopy
Author(s) :
Gigant, Benoît [Auteur]
Laboratoire d'enzymologie et biochimie structurales [LEBS]
Landrieu, Isabelle [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Fauquant, Caroline [Auteur]
Laboratoire d'enzymologie et biochimie structurales [LEBS]
Barbier, Pascale [Auteur]
Centre de Recherches en Oncologie biologique et Oncopharmacologie [CRO2]
Huvent, Isabelle [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Wieruszeski, Jean-Michel [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Knossow, Marcel [Auteur]
Laboratoire d'enzymologie et biochimie structurales [LEBS]
Lippens, Guy [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Laboratoire d'enzymologie et biochimie structurales [LEBS]
Landrieu, Isabelle [Auteur]

Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Fauquant, Caroline [Auteur]
Laboratoire d'enzymologie et biochimie structurales [LEBS]
Barbier, Pascale [Auteur]
Centre de Recherches en Oncologie biologique et Oncopharmacologie [CRO2]
Huvent, Isabelle [Auteur]

Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Wieruszeski, Jean-Michel [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Knossow, Marcel [Auteur]
Laboratoire d'enzymologie et biochimie structurales [LEBS]
Lippens, Guy [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Journal title :
Journal of the American Chemical Society
Volume number :
136
Pages :
12615-12623
Publication date :
2014-09-10
ISSN :
0002-7863, 1520-5126
HAL domain(s) :
Chimie/Chimie théorique et/ou physique
English abstract : [en]
Determining the molecular mechanism of the neuronal Tau protein in the tubulin heterodimer assembly has been a challenge owing to the dynamic character of the complex and the large size of microtubules. We use here defined ...
Show more >Determining the molecular mechanism of the neuronal Tau protein in the tubulin heterodimer assembly has been a challenge owing to the dynamic character of the complex and the large size of microtubules. We use here defined constructs comprising one or two tubulin heterodimers to characterize their association with a functional fragment of Tau, named TauF4. TauF4 binds with high affinities to the tubulin heterodimer complexes, but NMR spectroscopy shows that it remains highly dynamic, partly because of the interaction with the acidic C-terminal tails of the tubulin monomers. When bound to a single tubulin heterodimer, TauF4 is characterized by an overhanging peptide corresponding to the first of the four microtubule binding repeats of Tau. This peptide becomes immobilized in the complex with two longitudinally associated tubulin heterodimers. The longitudinal associations are favored by the fragment and contribute to Tau’s functional role in microtubule assembly.Show less >
Show more >Determining the molecular mechanism of the neuronal Tau protein in the tubulin heterodimer assembly has been a challenge owing to the dynamic character of the complex and the large size of microtubules. We use here defined constructs comprising one or two tubulin heterodimers to characterize their association with a functional fragment of Tau, named TauF4. TauF4 binds with high affinities to the tubulin heterodimer complexes, but NMR spectroscopy shows that it remains highly dynamic, partly because of the interaction with the acidic C-terminal tails of the tubulin monomers. When bound to a single tubulin heterodimer, TauF4 is characterized by an overhanging peptide corresponding to the first of the four microtubule binding repeats of Tau. This peptide becomes immobilized in the complex with two longitudinally associated tubulin heterodimers. The longitudinal associations are favored by the fragment and contribute to Tau’s functional role in microtubule assembly.Show less >
Language :
Anglais
Audience :
Non spécifiée
Administrative institution(s) :
CNRS
Université de Lille
Université de Lille
Research team(s) :
RMN et interactions moléculaires
Submission date :
2020-02-12T15:44:59Z
2021-03-10T08:51:44Z
2021-03-10T08:51:44Z