Thiol-based redox switches in eukaryotic proteins

Brandes, Nicolas; Schmitt, Sebastian; Jakob, Ursula

doi:10.1089/ars.2008.2285

Cited by 373Redox biology and oxidative stressSulfur Compounds in BiologyAntioxidant Activity and Oxidative Stress

Thiol-based redox switches in eukaryotic proteins

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Brandes, Nicolas, Schmitt, Sebastian, Jakob, Ursula·2009·Antioxidants & Redox Signaling

DOI 10.1089/ars.2008.2285PMC PMC2787739

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Abstract

For many years, oxidative thiol modifications in cytosolic proteins were largely disregarded as in vitro artifacts, and considered unlikely to play significant roles within the reducing environment of the cell. Recent developments in in vivo thiol trapping technology combined with mass spectrometric analysis have now provided convincing evidence that thiol-based redox switches are used as molecular tools in many proteins to regulate their activity in response to reactive oxygen and nitrogen species. Reversible oxidative thiol modifications have been found to modulate the function of proteins involved in many different pathways, starting from gene transcription, translation and protein folding, to metabolism, signal transduction, and ultimately apoptosis. This review will focus on three well-characterized eukaryotic proteins that use thiol-based redox switches to influence gene transcription, metabolism, and signal transduction. The transcription factor Yap1p is a good illustration of how oxidative modifications affect the function of a protein without changing its activity. We use glyeraldehyde-3-phosphate dehydrogenase to demonstrate how thiol modification of an active site cysteine re-routes metabolic pathways and converts a metabolic enzyme into a pro-apoptotic factor. Finally, we introduce the redox-sensitive protein tyrosine phosphatase PTP1B to illustrate that reversibility is one of the fundamental aspects of redox-regulation.

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Redox circuits involving glutathione and thioredoxin regulate insulin signaling molecules such as PTEN, SHIP2, and PTP1B.
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The low pKa of the catalytic cysteine allows it to act as a nucleophile for catalysis of dephosphorylation but also makes it a target for oxidation by ROS.
“The low pKa of this cysteine allows it to act as a nucleophile for catalysis of the dephosphorylation reaction, but also makes it a target for oxidation by ROS 6, 7.”
From Mitochondrial reactive oxygen species regulate cellular signaling and dictate biological outcomes (2010) · cites this paper as [7]
Oxidation of two intra- or intermolecular cysteines forms disulfide bridges allowing for conformational changes or oligomerization of proteins.
“Additionally, oxidation of two intra- or intermolecular cysteines forms disulfide bridges allowing for conformational changes or oligomerization of proteins 6, 7.”
From Mitochondrial reactive oxygen species regulate cellular signaling and dictate biological outcomes (2010) · cites this paper as [7]

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Authors: Brandes, N., Schmitt, S., & Jakob, U.
Affiliations: University of Michigan (US)
ORCID: Jakob, Ursula
Venue: Antioxidants & Redox Signaling
Publisher: SAGE Publications
Published: 2009-05
Volume: 11
Issue: 5
Pages: 997-1014
ISSN: 1523-0864 (ISSN-L)
1557-7716
DOI: 10.1089/ars.2008.2285
PMC: PMC2787739
OpenAlex: W2056357865
Cited by: 373
References: 156
Citations by year: 2026: 9 · 2025: 4 · 2024: 17 · 2023: 16 · 2022: 15 · 2021: 27 · 2020: 23 · 2019: 26 · 2018: 21 · 2017: 23 · 2016: 26 · 2015: 37 · 2014: 32 · 2013: 25 · 2012: 21
FWCI: 6.94
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Antioxidants and Redox Signaling (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Deep Blue (University of Michigan) (submittedVersion)
Funders: National Institute on Aging (R01AG027349)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Sulfur Compounds in Biology
Health Sciences › Medicine › Biochemistry › Antioxidant Activity and Oxidative Stress
Keywords: eukaryotic proteins, Yap1p, PTP1B, redox regulation, gene transcription, signal transduction, apoptosis, reactive oxygen species, reactive nitrogen species, cysteine modification
MeSH terms: Eukaryotic Cells, Oxidation-Reduction, Proteins, Sulfhydryl Compounds, Oxidative Stress

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Thiol-based redox switches in eukaryotic proteins

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