Glutathionylation of mitochondrial proteins.

TitleGlutathionylation of mitochondrial proteins.
Publication TypeJournal Article
Year of Publication2005
AuthorsHurd, TR, Costa, NJ, Dahm, CC, Beer, SM, Brown, SE, Filipovska, A, Murphy, MP
JournalAntioxid Redox Signal
Volume7
Issue7-8
Pagination999-1010
Date Published2005 Jul-Aug
ISSN1523-0864
KeywordsAnimals, Antioxidants, Glutathione, Humans, Mitochondrial Proteins, Oxidation-Reduction, Sulfhydryl Compounds, Thioredoxins
Abstract

Many proteins contain free thiols that can be modified by the reversible formation of mixed disulfides with low-molecular-weight thiols through a process called S-thiolation. As the majority of these modifications result from the interaction of protein thiols with the endogenous glutathione pool, protein glutathionylation is the predominant alteration. Protein glutathionylation is of significance both for defense against oxidative damage and in redox signaling. As mitochondria are at the heart of both oxidative damage and redox signaling within the cell, the glutathionylation of mitochondrial proteins is of particular importance. Here we review the mechanisms and physiological significance of the glutathionylation of mitochondrial thiol proteins.

DOI10.1089/ars.2005.7.999
Alternate JournalAntioxid. Redox Signal.
Citation Key10.1089/ars.2005.7.999
PubMed ID15998254