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Identification of a novel protein regulating microtubule stability through a chemical approach

Academic Article
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Overview

authors

  • Wignall, S. M.
  • Gray, N. S.
  • Chang, Y. T.
  • Juarez, L.
  • Jacob, R.
  • Burlingame, A.
  • Schultz, Peter
  • Heald, R.

publication date

  • January 2004

journal

  • Chemistry & Biology  Journal

abstract

  • To identify novel proteins regulating the microtubule cytoskeleton, we screened a library of purine derivatives using mitotic spindle assembly in Xenopus egg extracts as an assay. Out of a collection of 1561 compounds, we identified 15 that destabilized microtubules without targeting tubulin directly, resulting in small spindles. Affinity chromatography with one compound, named diminutol, revealed a potential target as NQO1, an NADP-dependent oxidoreductase. A role for NQO1 in influencing microtubule polymerization was confirmed through inhibition studies using known inhibitors and immunodepletion. Therefore, this chemical approach has identified a novel factor required for microtubule morphogenesis and cell division.

subject areas

  • Amino Acid Sequence
  • Animals
  • Cell Division
  • Chromosomes
  • Cytoskeleton
  • Enzyme Inhibitors
  • Gene Expression
  • Gene Library
  • Humans
  • Mice
  • Microtubule-Associated Proteins
  • Microtubules
  • Molecular Sequence Data
  • Molecular Structure
  • NAD(P)H Dehydrogenase (Quinone)
  • Phosphotransferases
  • Purines
  • Spindle Apparatus
  • Sulfides
  • Tubulin
  • Tubulin Modulators
  • Xenopus
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Identity

International Standard Serial Number (ISSN)

  • 1074-5521

Digital Object Identifier (DOI)

  • 10.1016/j.chembiol.2003.12.019

PubMed ID

  • 15113003
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Additional Document Info

start page

  • 135

end page

  • 146

volume

  • 11

issue

  • 1

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