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Tau-isoform dependent enhancement of taxol mobility through microtubules

Hyunjoo Park1, Mahnwon Kim, Deborah K Fygenson

  • 1Physics Department, Korea Advanced Institute of Science and Technology, Daejeon 305-701, Republic of Korea. phj78@kaist.ac.kr

Archives of Biochemistry and Biophysics
|August 12, 2008
PubMed

Insights

Different tau protein isoforms affect how taxol binds to microtubules. 3-repeat tau enhances taxol mobility more than 4-repeat tau, impacting drug interaction with microtubules.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Pharmacology

Background:

  • Microtubule-associated proteins (MAPs) like tau stabilize microtubules (MTs), regulating their dynamics.
  • Different tau isoforms, specifically 3-repeat and 4-repeat tau, exhibit varying efficacies in suppressing MT disassembly.

Purpose of the Study:

  • To investigate tau-isoform-dependent effects on taxol binding dynamics to microtubules.
  • To elucidate the mechanism by which tau isoforms influence taxol-MT interactions.

Main Methods:

  • Utilized fluorescence recovery after photobleaching (FRAP) assays.
  • Employed BODIPY-conjugated taxol bound to microtubules.
  • Measured taxol mobility under varying taxol concentrations in the presence of recombinant 3-repeat and 4-repeat tau.

Main Results:

  • Both 3-repeat and 4-repeat tau rendered taxol mobility highly sensitive to taxol concentration.
  • 3-repeat tau significantly accelerated taxol recovery (approx. 450s) at low concentrations (approx. 100 nM) compared to 4-repeat tau (approx. 1000s).
  • No change in taxol-MT binding affinity was observed, suggesting an alternative interaction mechanism.

Conclusions:

  • 3-repeat tau decreases the likelihood of taxol rebinding to its site within the microtubule lumen.
  • This effect is mediated either by direct competition for the taxol binding site (approx. 1 microM affinity) or by structural alterations in the microtubule facilitating taxol passage.

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