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Reference: Jung S, et al. (2010) Dynamic changes in the subcellular distribution of gpd1p in response to cell stress. J Biol Chem 285(9):6739-49

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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 role in redox balance. Here we show that Gpd1p is directed to peroxisomes by virtue of an amino-terminal type 2 peroxisomal targeting signal (PTS2) in a Pex7p-dependent manner. Significantly, Gpd1p(')s localization to peroxisomes is dependent on the metabolic status of cells and the phosphorylation of amino acyl 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 co-ordinately expressed with Gpd1p, and, under conditions of cell stress changes its subcellular distribution from peroxisomes to the nucleus where it mediates chromatin silencing. While peroxisomes are necessary for the beta-oxidation of fatty acids in yeast, the localization of Gpd1p to peroxisomes is not. Rather, alternate 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.

Reference Type
Journal Article
Authors
Jung S, Marelli M, Rachubinski RA, Goodlett DR, Aitchison JD
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