First tau repeat domain binding to growing and taxol-stabilized microtubules, and serine 262 residue phosphorylation.

Abstract:

:Tau phosphorylation plays a crucial role in microtubule stabilization and in Alzheimer's disease. To characterize the molecular mechanisms of tau binding on microtubules, we synthesized the peptide R1 (QTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQI), reproducing the first tau microtubule binding motif. We thermodynamically characterized the molecular mechanism of tubulin assembly with R1 in vitro, and measured, for the first time, the binding parameters of R1 on both growing and taxol-stabilized microtubules. In addition, we obtained similar binding parameters with R1 phosphorylated on Ser262. These data suggest that the consequences of Ser262 phosphorylation on tau binding to microtubules and on tubulin assembly are due to large intramolecular rearrangements of the tau protein.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Devred F,Douillard S,Briand C,Peyrot V

doi

10.1016/s0014-5793(02)02999-x

keywords:

subject

Has Abstract

pub_date

2002-07-17 00:00:00

pages

247-51

issue

1-3

eissn

0014-5793

issn

1873-3468

pii

S001457930202999X

journal_volume

523

pub_type

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