Paper
Methylglyoxal, a Metabolite Derived from Glycolysis, Functions as a Signal Initiator of the High Osmolarity Glycerol-Mitogen-activated Protein Kinase Cascade and Calcineurin/Crz1-mediated Pathway in Saccharomyces cerevisiae*
Published Jan 7, 2005 · Kazuhiro Maeta, S. Izawa, Y. Inoue
Journal of Biological Chemistry
110
Citations
2
Influential Citations
Abstract
Methylglyoxal (MG) is a typical 2-oxoaldehyde derived from glycolysis, although it inhibits the growth of cells in all types of organism. Hence, it has been questioned why such a toxic metabolite is synthesized via the ubiquitous energy-generating pathway. We have previously reported that expression of GLO1, coding for the major enzyme detoxifying MG, was induced by osmotic stress in a high osmolarity glycerol (HOG)-mitogen-activated protein (MAP) kinase-dependent manner in Saccharomyces cerevisiae. Here we show that MG activates the HOG-MAP kinase cascade. Two osmosensors, Sln1 and Sho1, have been identified to function upstream of the HOG-MAP kinase cascade, and we reveal that MG initiates the signal transduction to this MAP kinase cascade through the Sln1 branch. We also demonstrate that MG activates the Msn2 transcription factor. Moreover, MG activated the uptake of Ca2+ in yeast cells, thereby stimulating the calcineurin/Crz1-mediated Ca2+ signaling pathway. We propose that MG functions as a signal initiator in yeast.
In Vitro Study
Highly CitedMethylglyoxal, a toxic metabolite derived from glycolysis, activates the HOG-MAP kinase cascade and calcineurin/Crz1-mediated Ca2+ signaling pathway in yeast cells, suggesting its role as a signal initiator in
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