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Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation
Published on: June 21, 2021
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Global approaches for protein thiol redox state detection
Lisa R Knoke1, Lars I Leichert1
1Ruhr University Bochum, Institute of Biochemistry and Pathobiochemistry, Microbial Biochemistry, Universitätsstrasse 150, 44780 Bochum, Germany.
Current Opinion in Chemical Biology
|October 5, 2023
Summary
Cysteine
Area of Science:
- Biochemistry
- Molecular Biology
- Cellular Biology
Background:
- The thiol group of cysteine is highly nucleophilic and versatile.
- Cysteine residues are crucial for protein function, acting as active sites or forming disulfide bonds.
- Cytosolic cysteines are usually reduced but susceptible to oxidative modifications.
Purpose of the Study:
- To investigate the role of cysteine's oxidative post-translational modifications in redox regulation.
- To understand how these modifications impact protein function and cellular metabolism.
- To highlight the importance of studying these modifications in redox biology.
Main Methods:
- Proteomic analysis of cysteine oxidative post-translational modifications.
- Investigating the reversibility of these modifications in vivo.
- Studying the thioredoxin and glutaredoxin systems involved in thiol redox regulation.
Main Results:
- Oxidative modifications of cysteine are reversible in vivo.
- These modifications are linked to localized high oxidant levels.
- Thiol oxidation in regulatory proteins modulates cellular metabolism in response to oxidative stimuli.
Conclusions:
- Cysteine's oxidative post-translational modifications are key to thiol-based redox regulation.
- Understanding these modifications is essential for comprehending cellular responses to oxidative stress.
- Proteomic studies are indispensable for advancing redox biology research.
