Pyruvate kinase as a microtubule destabilizing factor in vitro

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Endogenous control of microtubule dynamism is essential in many cell types. Numerous microtubule-adhering proteins stabilize the polymer status, while very few protein factors are described with opposite effects. The brain- and muscle-specific M1 isoform of the enzyme pyruvate kinase is investigated here in this respect. Three pieces of evidence indicate antimicrotubular effects of this protein. (1) Pyruvate kinase inhibits taxol-induced tubulin polymerization into microtubules as revealed by turbidimetry. (2) Pelleting experiments show that pyruvate kinase partially disassembles taxol-stabilized microtubules into less sedimentable oligomers leading to the appearance of tubulin in the supernatant fractions. (3) Electron microscopy reveals the kinase-induced formation of great amounts of thread-like tubulin oligomers which tend to accumulate in a light/less sedimentable fraction. Immunoelectron micrographs using labeled antibody against pyruvate kinase provide evidence for the binding of pyruvate kinase to the thread-like oligomeric forms. The present data allow the assumption that pyruvate kinase may display multiple regulatory functions as a glycolytic control enzyme and as a modulator of microtubule dynamism.

Original languageEnglish
Pages (from-to)430-435
Number of pages6
JournalBiochemical and biophysical research communications
Issue number2
Publication statusPublished - Jan 19 1999


  • Differential pelleting
  • Microtubule antagonism
  • Microtubule dynamism
  • Microtubule ultrastructure
  • Pyruvate kinase
  • Turbidimetry

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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