Redox control of eukaryotic secretion by a novel pathway regulating the ER import of glutathione

A. Ponsero; A. Igbaria; M. Darch; S. Miled; C. Outten; J. Winther; G. Palais; B. D'autreaux; A. Delaunay-Moisan; M. B. Toledano

doi:https://doi.org/10.1111/febs.14172

Redox control of eukaryotic secretion by a novel pathway regulating the ER import of glutathione

A. Ponsero, A. Igbaria, M. Darch, S. Miled, C. Outten, J. Winther, G. Palais, B. D'autreaux, A. Delaunay-Moisan, M. B. Toledano

Department of Life Sciences

Ben-Gurion University of the Negev

Research output: Contribution to journal › Meeting Abstract › peer-review

Abstract

Disturbance of glutathione metabolism is a hallmark of numerous diseases, yet glutathione functions are still poorly under-stood. One key to address this question is to consider its functional compartmentation. In the endoplasmic reticulum(ER), protein folding requires disulﬁde bond formation catalyzed by the thiol oxidase Ero1 and protein disulﬁde isomerase (PDI).In the ER, glutathione is thought to counterbalance ER oxidation by the Ero1-PDI redox relay, which explain its relative more oxidized redox state (EGSH -242 mV), relative to the cytoplasm(EGSH = -295 mV)

Original language	American English
Article number	S.3.3.A-003
Pages (from-to)	30-30
Number of pages	1
Journal	FEBS Journal
Volume	284
DOIs	https://doi.org/10.1111/febs.14172
State	Published - Sep 2017

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https://doi.org/10.1111/febs.14172

Cite this

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title = "Redox control of eukaryotic secretion by a novel pathway regulating the ER import of glutathione",

abstract = "Disturbance of glutathione metabolism is a hallmark of numerous diseases, yet glutathione functions are still poorly under-stood. One key to address this question is to consider its functional compartmentation. In the endoplasmic reticulum(ER), protein folding requires disulﬁde bond formation catalyzed by the thiol oxidase Ero1 and protein disulﬁde isomerase (PDI).In the ER, glutathione is thought to counterbalance ER oxidation by the Ero1-PDI redox relay, which explain its relative more oxidized redox state (EGSH -242 mV), relative to the cytoplasm(EGSH = -295 mV)",

author = "A. Ponsero and A. Igbaria and M. Darch and S. Miled and C. Outten and J. Winther and G. Palais and B. D'autreaux and A. Delaunay-Moisan and Toledano, {M. B.}",

note = "42nd FEBS Congress, From Molecules to Cells and Back, Jerusalem, Israel, September 10-14, 2017",

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doi = "https://doi.org/10.1111/febs.14172",

language = "American English",

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journal = "FEBS Journal",

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TY - JOUR

T1 - Redox control of eukaryotic secretion by a novel pathway regulating the ER import of glutathione

AU - Ponsero, A.

AU - Igbaria, A.

AU - Darch, M.

AU - Miled, S.

AU - Outten, C.

AU - Winther, J.

AU - Palais, G.

AU - D'autreaux, B.

AU - Delaunay-Moisan, A.

AU - Toledano, M. B.

N1 - 42nd FEBS Congress, From Molecules to Cells and Back, Jerusalem, Israel, September 10-14, 2017

PY - 2017/9

Y1 - 2017/9

N2 - Disturbance of glutathione metabolism is a hallmark of numerous diseases, yet glutathione functions are still poorly under-stood. One key to address this question is to consider its functional compartmentation. In the endoplasmic reticulum(ER), protein folding requires disulﬁde bond formation catalyzed by the thiol oxidase Ero1 and protein disulﬁde isomerase (PDI).In the ER, glutathione is thought to counterbalance ER oxidation by the Ero1-PDI redox relay, which explain its relative more oxidized redox state (EGSH -242 mV), relative to the cytoplasm(EGSH = -295 mV)

AB - Disturbance of glutathione metabolism is a hallmark of numerous diseases, yet glutathione functions are still poorly under-stood. One key to address this question is to consider its functional compartmentation. In the endoplasmic reticulum(ER), protein folding requires disulﬁde bond formation catalyzed by the thiol oxidase Ero1 and protein disulﬁde isomerase (PDI).In the ER, glutathione is thought to counterbalance ER oxidation by the Ero1-PDI redox relay, which explain its relative more oxidized redox state (EGSH -242 mV), relative to the cytoplasm(EGSH = -295 mV)

U2 - https://doi.org/10.1111/febs.14172

DO - https://doi.org/10.1111/febs.14172

M3 - Meeting Abstract

SN - 1742-464X

VL - 284

SP - 30

EP - 30

JO - FEBS Journal

JF - FEBS Journal

M1 - S.3.3.A-003

ER -