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 Lettjournal_title
FEBS lettersauthors
Devred F,Douillard S,Briand C,Peyrot Vdoi
10.1016/s0014-5793(02)02999-xkeywords:
subject
Has Abstractpub_date
2002-07-17 00:00:00pages
247-51issue
1-3eissn
0014-5793issn
1873-3468pii
S001457930202999Xjournal_volume
523pub_type
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