The yeast oligopeptide transporter Opt2 is localized to peroxisomes and affects glutathione redox homeostasis
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The yeast oligopeptide transporter Opt2 is localized to peroxisomes and affects glutathione redox homeostasis. / Elbaz-Alon, Yael; Morgan, Bruce; Clancy, Anne; Amoako, Theresa N E; Zalckvar, Einat; Dick, Tobias P; Schwappach, Blanche; Schuldiner, Maya.
In: FEMS YEAST RES, Vol. 14, No. 7, 11.2014, p. 1055-67.Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review
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TY - JOUR
T1 - The yeast oligopeptide transporter Opt2 is localized to peroxisomes and affects glutathione redox homeostasis
AU - Elbaz-Alon, Yael
AU - Morgan, Bruce
AU - Clancy, Anne
AU - Amoako, Theresa N E
AU - Zalckvar, Einat
AU - Dick, Tobias P
AU - Schwappach, Blanche
AU - Schuldiner, Maya
N1 - © 2014 Federation of European Microbiological Societies. Published by John Wiley & Sons Ltd. All rights reserved.
PY - 2014/11
Y1 - 2014/11
N2 - Glutathione, the most abundant small-molecule thiol in eukaryotic cells, is synthesized de novo solely in the cytosol and must subsequently be transported to other cellular compartments. The mechanisms of glutathione transport into and out of organelles remain largely unclear. We show that budding yeast Opt2, a close homolog of the plasma membrane glutathione transporter Opt1, localizes to peroxisomes. We demonstrate that deletion of OPT2 leads to major defects in maintaining peroxisomal, mitochondrial, and cytosolic glutathione redox homeostasis. Furthermore, ∆opt2 strains display synthetic lethality with deletions of genes central to iron homeostasis that require mitochondrial glutathione redox homeostasis. Our results shed new light on the importance of peroxisomes in cellular glutathione homeostasis.
AB - Glutathione, the most abundant small-molecule thiol in eukaryotic cells, is synthesized de novo solely in the cytosol and must subsequently be transported to other cellular compartments. The mechanisms of glutathione transport into and out of organelles remain largely unclear. We show that budding yeast Opt2, a close homolog of the plasma membrane glutathione transporter Opt1, localizes to peroxisomes. We demonstrate that deletion of OPT2 leads to major defects in maintaining peroxisomal, mitochondrial, and cytosolic glutathione redox homeostasis. Furthermore, ∆opt2 strains display synthetic lethality with deletions of genes central to iron homeostasis that require mitochondrial glutathione redox homeostasis. Our results shed new light on the importance of peroxisomes in cellular glutathione homeostasis.
KW - Gene Deletion
KW - Glutathione/metabolism
KW - Homeostasis
KW - Membrane Transport Proteins/analysis
KW - Oligopeptides/metabolism
KW - Oxidation-Reduction
KW - Peroxisomes/chemistry
KW - Saccharomyces cerevisiae/enzymology
KW - Saccharomyces cerevisiae Proteins/analysis
U2 - 10.1111/1567-1364.12196
DO - 10.1111/1567-1364.12196
M3 - SCORING: Journal article
C2 - 25130273
VL - 14
SP - 1055
EP - 1067
IS - 7
ER -