Discodermolide interferes with the binding of tau protein to microtubules

FEBS Letters

Amos, Linda A²  Paterson, Ian¹  Florence, Gordon J¹  Kar, Santwana² 

[1] University of Cambridge, Univ Chem Lab, Lensfield Rd, Cambridge CB2 1EW, UK;MRC Laboratory of Molecular Biology, Hills Rd, Cambridge CB2 2QH, UK

关键词: Tubulin;    Tau;    Microtubule-associated protein;    Discodermolide;    Taxol;    MAP;    microtubule-associated protein;    TMAO;    trimethylamine-N-oxide;    DMSO;    dimethyl sulphoxide;   

DOI  :  10.1016/S0014-5793(03)00181-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We investigated whether discodermolide, a novel antimitotic agent, affects the binding to microtubules of tau protein repeat motifs. Like taxol, the new drug reduces the proportion of tau that pellets with microtubules. Despite their differing structures, discodermolide, taxol and tau repeats all bind to a site on β-tubulin that lies within the microtubule lumen and is crucial in controlling microtubule assembly. Low concentrations of tau still bind strongly to the outer surfaces of preformed microtubules when the acidic C-terminal regions of at least six tubulin dimers are available for interaction with each tau molecule; otherwise binding is very weak.

【 授权许可】

Unknown