The glucose-induced polyphosphoinositides turnover in Saccharomyces cerevisiae is not dependent on the CDC25-RAS mediated signal transduction pathway

FEBS Lett. 1990 Nov 12;274(1-2):19-22. doi: 10.1016/0014-5793(90)81319-j.

Abstract

Recently the polyphosphoinositides (PI) turnover has been related to the control of growth and cell cycle also in Saccharomyces cerevisiae, and the RAS2 and RAS1 gene products have been shown to be involved in the stimulation of PI turnover in G0/G1 arrested yeast cells. Here we show that addition of glucose to previously glucose-starved cells, stimulates, the PI turnover with fast kinetics also in yeast cells that were not arrested in the G0/G1 phase of the cell cycle. In addition PI turnover is equally stimulated in temperature sensitive cdc25-1 and cdc25-5 strains at restrictive temperature, as well as in ras1, ras2-ts strain, suggesting that PI turnover stimulation is not dependent on the CDC25-RAS mediated signal transduction pathway.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Cycle Proteins*
  • Fungal Proteins / metabolism*
  • GTP-Binding Proteins / physiology
  • Galactose / metabolism
  • Genotype
  • Glucose / metabolism*
  • Glucose / pharmacology
  • Kinetics
  • Phosphatidylinositol Phosphates
  • Phosphatidylinositols / metabolism*
  • Phospholipids / isolation & purification
  • Phospholipids / metabolism
  • Saccharomyces cerevisiae / drug effects
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / metabolism*
  • Saccharomyces cerevisiae Proteins*
  • Signal Transduction*
  • ras Proteins*
  • ras-GRF1*

Substances

  • CDC25 protein, S cerevisiae
  • Cell Cycle Proteins
  • Fungal Proteins
  • Phosphatidylinositol Phosphates
  • Phosphatidylinositols
  • Phospholipids
  • Saccharomyces cerevisiae Proteins
  • ras-GRF1
  • GTP-Binding Proteins
  • RAS1 protein, S cerevisiae
  • RAS2 protein, S cerevisiae
  • ras Proteins
  • Glucose
  • Galactose