Pyruvate kinase as a microtubule destabilizing factor in vitro

Research output: Contribution to journalArticle

28 Citations (Scopus)

Abstract

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
Volume254
Issue number2
DOIs
Publication statusPublished - Jan 19 1999

Fingerprint

Pyruvate Kinase
Microtubules
Tubulin
Paclitaxel
Oligomers
Tubulin Modulators
Nephelometry and Turbidimetry
Microtubule Proteins
Pelletizing
Proteins
Enzymes
Polymerization
Electron microscopy
Muscle
In Vitro Techniques
Brain
Electron Microscopy
Polymers
Protein Isoforms
Phosphotransferases

Keywords

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

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Pyruvate kinase as a microtubule destabilizing factor in vitro. / Vértessy, B.; Bánkfalvi, Dóra; Kovács, J.; Lőw, P.; Lehotzky, A.; Ovádi, J.

In: Biochemical and Biophysical Research Communications, Vol. 254, No. 2, 19.01.1999, p. 430-435.

Research output: Contribution to journalArticle

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