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Discodermolide interferes with the binding of tau protein to microtubules
Author(s) -
Kar Santwana,
Florence Gordon J,
Paterson Ian,
Amos Linda A
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)00181-9
Subject(s) - microtubule , tubulin , chemistry , biophysics , tau protein , binding site , microtubule associated protein , plasma protein binding , microbiology and biotechnology , biochemistry , biology , medicine , disease , pathology , alzheimer's disease
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.