Protein S-glutathionylation: The linchpin for the transmission of regulatory information on redox buffering capacity in mitochondria.
Identifieur interne : 000132 ( Main/Exploration ); précédent : 000131; suivant : 000133Protein S-glutathionylation: The linchpin for the transmission of regulatory information on redox buffering capacity in mitochondria.
Auteurs : Adrian Young [Canada] ; Robert Gill [Canada] ; Ryan J. Mailloux [Canada]Source :
- Chemico-biological interactions [ 1872-7786 ] ; 2019.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Antioxydants (métabolisme), Dynamique mitochondriale (MeSH), Espèces réactives de l'oxygène (métabolisme), Glutarédoxines (métabolisme), Glutathion (métabolisme), Glutathione transferase (métabolisme), Mitochondries (métabolisme), Phosphorylation oxydative (MeSH), Protéines mitochondriales (métabolisme).
- MESH :
English descriptors
- KwdEn :
- Animals (MeSH), Antioxidants (metabolism), Glutaredoxins (metabolism), Glutathione (metabolism), Glutathione Transferase (metabolism), Mitochondria (metabolism), Mitochondrial Dynamics (MeSH), Mitochondrial Proteins (metabolism), Oxidative Phosphorylation (MeSH), Reactive Oxygen Species (metabolism).
- MESH :
- chemical , metabolism : Antioxidants, Glutaredoxins, Glutathione, Glutathione Transferase, Mitochondrial Proteins, Reactive Oxygen Species.
- metabolism : Mitochondria.
- Animals, Mitochondrial Dynamics, Oxidative Phosphorylation.
Abstract
Protein S-glutathionylation reactions are a ubiquitous oxidative modification required to control protein function in response to changes in redox buffering capacity. These reactions are rapid and reversible and are, for the most part, enzymatically mediated by glutaredoxins (GRX) and glutathione S-transferases (GST). Protein S-glutathionylation has been found to control a range of cell functions in response to different physiological cues. Although these reactions occur throughout the cell, mitochondrial proteins seem to be highly susceptible to reversible S-glutathionylation, a feature attributed to the unique physical properties of this organelle. Indeed, mitochondria contain a number of S-glutathionylation targets which includes proteins involved in energy metabolism, solute transport, reactive oxygen species (ROS) production, proton leaks, apoptosis, antioxidant defense, and mitochondrial fission and fusion. Moreover, it has been found that conjugation and removal of glutathione from proteins in mitochondria fulfills a number of important physiological roles and defects in these reactions can have some dire pathological consequences. Here, we provide an updated overview on mitochondrial protein S-glutathionylation reactions and their importance in cell functions and physiology.
DOI: 10.1016/j.cbi.2018.12.003
PubMed: 30537466
Affiliations:
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Electronic address: rjmailloux@mun.ca.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Department of Biochemistry, Faculty of Science, Memorial University of Newfoundland, St. John's, NL</wicri:regionArea><wicri:noRegion>NL</wicri:noRegion></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2019">2019</date><idno type="RBID">pubmed:30537466</idno><idno type="pmid">30537466</idno><idno type="doi">10.1016/j.cbi.2018.12.003</idno><idno type="wicri:Area/Main/Corpus">000187</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000187</idno><idno type="wicri:Area/Main/Curation">000187</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000187</idno><idno type="wicri:Area/Main/Exploration">000187</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Protein S-glutathionylation: The linchpin for the transmission of regulatory information on redox buffering capacity in mitochondria.</title><author><name sortKey="Young, Adrian" sort="Young, Adrian" uniqKey="Young A" first="Adrian" last="Young">Adrian Young</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry, Faculty of Science, Memorial University of Newfoundland, St. John's, NL, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Department of Biochemistry, Faculty of Science, Memorial University of Newfoundland, St. John's, NL</wicri:regionArea><wicri:noRegion>NL</wicri:noRegion></affiliation></author><author><name sortKey="Gill, Robert" sort="Gill, Robert" uniqKey="Gill R" first="Robert" last="Gill">Robert Gill</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry, Faculty of Science, Memorial University of Newfoundland, St. John's, NL, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Department of Biochemistry, Faculty of Science, Memorial University of Newfoundland, St. John's, NL</wicri:regionArea><wicri:noRegion>NL</wicri:noRegion></affiliation></author><author><name sortKey="Mailloux, Ryan J" sort="Mailloux, Ryan J" uniqKey="Mailloux R" first="Ryan J" last="Mailloux">Ryan J. Mailloux</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry, Faculty of Science, Memorial University of Newfoundland, St. John's, NL, Canada. Electronic address: rjmailloux@mun.ca.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Department of Biochemistry, Faculty of Science, Memorial University of Newfoundland, St. John's, NL</wicri:regionArea><wicri:noRegion>NL</wicri:noRegion></affiliation></author></analytic><series><title level="j">Chemico-biological interactions</title><idno type="eISSN">1872-7786</idno><imprint><date when="2019" type="published">2019</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term><term>Antioxidants (metabolism)</term><term>Glutaredoxins (metabolism)</term><term>Glutathione (metabolism)</term><term>Glutathione Transferase (metabolism)</term><term>Mitochondria (metabolism)</term><term>Mitochondrial Dynamics (MeSH)</term><term>Mitochondrial Proteins (metabolism)</term><term>Oxidative Phosphorylation (MeSH)</term><term>Reactive Oxygen Species (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Antioxydants (métabolisme)</term><term>Dynamique mitochondriale (MeSH)</term><term>Espèces réactives de l'oxygène (métabolisme)</term><term>Glutarédoxines (métabolisme)</term><term>Glutathion (métabolisme)</term><term>Glutathione transferase (métabolisme)</term><term>Mitochondries (métabolisme)</term><term>Phosphorylation oxydative (MeSH)</term><term>Protéines mitochondriales (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Antioxidants</term><term>Glutaredoxins</term><term>Glutathione</term><term>Glutathione Transferase</term><term>Mitochondrial Proteins</term><term>Reactive Oxygen Species</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Mitochondria</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Antioxydants</term><term>Espèces réactives de l'oxygène</term><term>Glutarédoxines</term><term>Glutathion</term><term>Glutathione transferase</term><term>Mitochondries</term><term>Protéines mitochondriales</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Mitochondrial Dynamics</term><term>Oxidative Phosphorylation</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Dynamique mitochondriale</term><term>Phosphorylation oxydative</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Protein S-glutathionylation reactions are a ubiquitous oxidative modification required to control protein function in response to changes in redox buffering capacity. These reactions are rapid and reversible and are, for the most part, enzymatically mediated by glutaredoxins (GRX) and glutathione S-transferases (GST). Protein S-glutathionylation has been found to control a range of cell functions in response to different physiological cues. Although these reactions occur throughout the cell, mitochondrial proteins seem to be highly susceptible to reversible S-glutathionylation, a feature attributed to the unique physical properties of this organelle. Indeed, mitochondria contain a number of S-glutathionylation targets which includes proteins involved in energy metabolism, solute transport, reactive oxygen species (ROS) production, proton leaks, apoptosis, antioxidant defense, and mitochondrial fission and fusion. Moreover, it has been found that conjugation and removal of glutathione from proteins in mitochondria fulfills a number of important physiological roles and defects in these reactions can have some dire pathological consequences. Here, we provide an updated overview on mitochondrial protein S-glutathionylation reactions and their importance in cell functions and physiology.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">30537466</PMID><DateCompleted><Year>2019</Year><Month>02</Month><Day>04</Day></DateCompleted><DateRevised><Year>2019</Year><Month>02</Month><Day>15</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1872-7786</ISSN><JournalIssue CitedMedium="Internet"><Volume>299</Volume><PubDate><Year>2019</Year><Month>Feb</Month><Day>01</Day></PubDate></JournalIssue><Title>Chemico-biological interactions</Title><ISOAbbreviation>Chem Biol Interact</ISOAbbreviation></Journal><ArticleTitle>Protein S-glutathionylation: The linchpin for the transmission of regulatory information on redox buffering capacity in mitochondria.</ArticleTitle><Pagination><MedlinePgn>151-162</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0009-2797(18)31097-4</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.cbi.2018.12.003</ELocationID><Abstract><AbstractText>Protein S-glutathionylation reactions are a ubiquitous oxidative modification required to control protein function in response to changes in redox buffering capacity. These reactions are rapid and reversible and are, for the most part, enzymatically mediated by glutaredoxins (GRX) and glutathione S-transferases (GST). Protein S-glutathionylation has been found to control a range of cell functions in response to different physiological cues. Although these reactions occur throughout the cell, mitochondrial proteins seem to be highly susceptible to reversible S-glutathionylation, a feature attributed to the unique physical properties of this organelle. Indeed, mitochondria contain a number of S-glutathionylation targets which includes proteins involved in energy metabolism, solute transport, reactive oxygen species (ROS) production, proton leaks, apoptosis, antioxidant defense, and mitochondrial fission and fusion. Moreover, it has been found that conjugation and removal of glutathione from proteins in mitochondria fulfills a number of important physiological roles and defects in these reactions can have some dire pathological consequences. Here, we provide an updated overview on mitochondrial protein S-glutathionylation reactions and their importance in cell functions and physiology.</AbstractText><CopyrightInformation>Copyright © 2018. Published by Elsevier B.V.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Young</LastName><ForeName>Adrian</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, Faculty of Science, Memorial University of Newfoundland, St. John's, NL, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Gill</LastName><ForeName>Robert</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, Faculty of Science, Memorial University of Newfoundland, St. John's, NL, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mailloux</LastName><ForeName>Ryan J</ForeName><Initials>RJ</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, Faculty of Science, Memorial University of Newfoundland, St. John's, NL, Canada. 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