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Quantitative Analysis of Tau-Microtubule Interaction Using FRET

Aix-Marseille Université, Inserm, CRO2 UMR_S 911, Faculté de Pharmacie, 27 Bd Jean Moulin, 13385 Marseille, France
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2014, 15(8), 14697-14714;
Received: 23 May 2014 / Revised: 30 June 2014 / Accepted: 14 July 2014 / Published: 21 August 2014
(This article belongs to the Special Issue Förster Resonance Energy Transfer (FRET) 2015)
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The interaction between the microtubule associated protein, tau and the microtubules is investigated. A fluorescence resonance energy transfer (FRET) assay was used to determine the distance separating tau to the microtubule wall, as well as the binding parameters of the interaction. By using microtubules stabilized with Flutax-2 as donor and tau labeled with rhodamine as acceptor, a donor-to-acceptor distance of 54 ± 1 Å was found. A molecular model is proposed in which Flutax-2 is directly accessible to tau-rhodamine molecules for energy transfer. By titration, we calculated the stoichiometric dissociation constant to be equal to 1.0 ± 0.5 µM. The influence of the C-terminal tails of αβ-tubulin on the tau-microtubule interaction is presented once a procedure to form homogeneous solution of cleaved tubulin has been determined. The results indicate that the C-terminal tails of α- and β-tubulin by electrostatic effects and of recruitment seem to be involved in the binding mechanism of tau. View Full-Text
Keywords: tau; microtubules; FRET; energy transfer; interaction tau; microtubules; FRET; energy transfer; interaction

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This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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Maïo, I.L.D.; Barbier, P.; Allegro, D.; Brault, C.; Peyrot, V. Quantitative Analysis of Tau-Microtubule Interaction Using FRET. Int. J. Mol. Sci. 2014, 15, 14697-14714.

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