Abstract

Gpd1p is a cytosolic NAD(+)-dependent glycerol 3-phosphate dehydrogenase that also localizes to peroxisomes and plays an essential role in the cellular response to osmotic stress and a role in redox balance. Here, we show that Gpd1p is directed to peroxisomes by virtue of an N-terminal type 2 peroxisomal targeting signal (PTS2) in a Pex7p-dependent manner. Significantly, localization of Gpd1p to peroxisomes is dependent on the metabolic status of cells and the phosphorylation of aminoacyl residues adjacent to the targeting signal. Exposure of cells to osmotic stress induces changes in the subcellular distribution of Gpd1p to the cytosol and nucleus. This behavior is similar to Pnc1p, which is coordinately expressed with Gpd1p, and under conditions of cell stress changes its subcellular distribution from peroxisomes to the nucleus where it mediates chromatin silencing. Although peroxisomes are necessary for the beta-oxidation of fatty acids in yeast, the localization of Gpd1p to peroxisomes is not. Rather, shifts in the distribution of Gpd1p to different cellular compartments in response to changing cellular status suggests a role for Gpd1p in the spatial regulation of redox potential, a process critical to cell survival, especially under the complex stress conditions expected to occur in the wild.

Highlights

  • Glycerol 3-phosphate dehydrogenase (Gpd1p) is one of two NADϩ-dependent glycerol 3-phosphate dehydrogenases in yeast [1, 2]

  • We found that Gpd1p dynamically changes its subcellular distribution among the cytosol, peroxisome, and nucleus depending on the type of cellular stress, becoming primarily peroxisomal upon exposure to the fatty acid, oleic acid, and nucleus upon exposure to osmotic stress

  • Are peroxisomes, Gpd1p-mCherry was co-localized with Pex13p-GFP, an abundant peroxisomal membrane protein in cells grown in glucose (Fig. 1D)

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Summary

Introduction

Glycerol 3-phosphate dehydrogenase (Gpd1p) is one of two NADϩ-dependent glycerol 3-phosphate dehydrogenases in yeast [1, 2]. This behavior is similar to Pnc1p, which is coordinately expressed with Gpd1p, and under conditions of cell stress changes its subcellular distribution from peroxisomes to the nucleus where it mediates chromatin silencing.

Results
Conclusion

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