Taxol

A new probe for studying the structure and function of microtubules

Susan Band Horwitz, J. Parness, P. B. Schiff, J. J. Manfredi

Research output: Contribution to journalArticle

54 Citations (Scopus)

Abstract

Taxol has the capacity to shift the equilibrium between the tubulin dimer and polymer in favor of the microtubule in an in vitro assembly system. The drug decreases dramatically the critical concentration of microtubule protein (MTO, tubulin plus microtubulin-associated proteins) required for microtubule assembly. Microtubules assembled in the presence of taxol are stable to polymerization by 4 mM CaCl2 and by a fivefold dilution, but they can be slowly depolymerized by podophyllotoxin or vinblastine. Taxol is unusual, compared with other small molecules such as colchicine, in its ability to bind efficiently to the assembled stead-state microtubule. Examination of the binding of taxol to cells growing in tissue culture has resulted in data that correlate well with our knowledge of the interaction of the drug with microtubules in vitro.

Original languageEnglish (US)
Pages (from-to)219-226
Number of pages8
JournalCold Spring Harbor Symposia on Quantitative Biology
Volume46
Issue number1
StatePublished - 1982

Fingerprint

paclitaxel
Paclitaxel
Microtubules
microtubules
Tubulin
Podophyllotoxin
Microtubule Proteins
tubulin
Tissue culture
Microtubule-Associated Proteins
Vinblastine
Colchicine
Drug Interactions
Polymerization
Pharmaceutical Preparations
Dimers
Dilution
vinblastine
drug interactions
Polymers

ASJC Scopus subject areas

  • Agricultural and Biological Sciences(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Molecular Biology

Cite this

Taxol : A new probe for studying the structure and function of microtubules. / Band Horwitz, Susan; Parness, J.; Schiff, P. B.; Manfredi, J. J.

In: Cold Spring Harbor Symposia on Quantitative Biology, Vol. 46, No. 1, 1982, p. 219-226.

Research output: Contribution to journalArticle

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