Discodermolide interferes with the binding of tau protein to microtubules

Santwana Kar, Gordon John Florence, Ian Paterson, Linda A. Amos

Research output: Contribution to journalArticlepeer-review

34 Citations (Scopus)

Abstract

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 beta-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. (C) 2003 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.

Original languageEnglish
Pages (from-to)34-36
Number of pages3
JournalFEBS Letters
Volume539
Issue number1-3
DOIs
Publication statusPublished - 27 Mar 2003

Keywords

  • tubulin
  • tau
  • microtubule-associated protein
  • discodermolide
  • taxol
  • TRIMETHYLAMINE-N-OXIDE
  • ALPHA-BETA-TUBULIN
  • TAXOL-BINDING
  • RESOLUTION
  • (+)-DISCODERMOLIDE
  • CONFORMATION
  • SUBTILISIN
  • ANGSTROM
  • DOMAINS
  • AGENT

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