The yeast oligopeptide transporter Opt2 is localized to peroxisomes and affects glutathione redox homeostasis

Yael Elbaz-Alon; Bruce Morgan; Anne Clancy; Theresa N E Amoako; Einat Zalckvar; Tobias P Dick; Blanche Schwappach; Maya Schuldiner

doi:10.1111/1567-1364.12196

The yeast oligopeptide transporter Opt2 is localized to peroxisomes and affects glutathione redox homeostasis

Standard

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, Jahrgang 14, Nr. 7, 11.2014, S. 1055-67.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Elbaz-Alon, Y, Morgan, B, Clancy, A, Amoako, TNE, Zalckvar, E, Dick, TP, Schwappach, B & Schuldiner, M 2014, 'The yeast oligopeptide transporter Opt2 is localized to peroxisomes and affects glutathione redox homeostasis', FEMS YEAST RES, Jg. 14, Nr. 7, S. 1055-67. https://doi.org/10.1111/1567-1364.12196

APA

Elbaz-Alon, Y., Morgan, B., Clancy, A., Amoako, T. N. E., Zalckvar, E., Dick, T. P., Schwappach, B., & Schuldiner, M. (2014). The yeast oligopeptide transporter Opt2 is localized to peroxisomes and affects glutathione redox homeostasis. FEMS YEAST RES, 14(7), 1055-67. https://doi.org/10.1111/1567-1364.12196

Vancouver

Elbaz-Alon Y, Morgan B, Clancy A, Amoako TNE, Zalckvar E, Dick TP et al. The yeast oligopeptide transporter Opt2 is localized to peroxisomes and affects glutathione redox homeostasis. FEMS YEAST RES. 2014 Nov;14(7):1055-67. https://doi.org/10.1111/1567-1364.12196

Bibtex

@article{a177dfeef6904bb8b73c89371d14cab0,

title = "The yeast oligopeptide transporter Opt2 is localized to peroxisomes and affects glutathione redox homeostasis",

abstract = "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. ",

keywords = "Gene Deletion, Glutathione/metabolism, Homeostasis, Membrane Transport Proteins/analysis, Oligopeptides/metabolism, Oxidation-Reduction, Peroxisomes/chemistry, Saccharomyces cerevisiae/enzymology, Saccharomyces cerevisiae Proteins/analysis",

author = "Yael Elbaz-Alon and Bruce Morgan and Anne Clancy and Amoako, {Theresa N E} and Einat Zalckvar and Dick, {Tobias P} and Blanche Schwappach and Maya Schuldiner",

year = "2014",

month = nov,

doi = "10.1111/1567-1364.12196",

language = "English",

volume = "14",

pages = "1055--67",

number = "7",

}

RIS

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

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 -