Cytosolic redox components regulate protein homeostasis via additional localisation in the mitochondrial intermembrane space.
Identifieur interne : 000377 ( Main/Exploration ); précédent : 000376; suivant : 000378Cytosolic redox components regulate protein homeostasis via additional localisation in the mitochondrial intermembrane space.
Auteurs : Mauricio Cardenas-Rodriguez [Royaume-Uni] ; Kostas Tokatlidis [Royaume-Uni]Source :
- FEBS letters [ 1873-3468 ] ; 2017.
Descripteurs français
- KwdFr :
- MESH :
- composition chimique : Protéines.
- métabolisme : Cytosol, Membranes mitochondriales, Protéines.
- Animaux, Humains, Oxydoréduction, Pliage des protéines, Transport des protéines.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Proteins.
- metabolism : Cytosol, Mitochondrial Membranes, Proteins.
- Animals, Humans, Oxidation-Reduction, Protein Folding, Protein Transport.
Abstract
Oxidative protein folding is confined to the bacterial periplasm, endoplasmic reticulum and the mitochondrial intermembrane space. Maintaining a redox balance requires the presence of reductive pathways. The major thiol-reducing pathways engage the thioredoxin and the glutaredoxin systems which are involved in removal of oxidants, protein proofreading and folding. Alterations in redox balance likely affect the flux of these redox pathways and are related to ageing and diseases such as neurodegenerative disorders and cancer. Here, we first review the well-studied oxidative and reductive processes in the bacterial periplasm and the endoplasmic reticulum, and then discuss the less understood process in the mitochondrial intermembrane space, highlighting its importance for the proper function of the cell.
DOI: 10.1002/1873-3468.12766
PubMed: 28746987
PubMed Central: PMC5601281
Affiliations:
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de Glasgow</orgName></affiliation></author></analytic><series><title level="j">FEBS letters</title><idno type="eISSN">1873-3468</idno><imprint><date when="2017" type="published">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term><term>Cytosol (metabolism)</term><term>Humans (MeSH)</term><term>Mitochondrial Membranes (metabolism)</term><term>Oxidation-Reduction (MeSH)</term><term>Protein Folding (MeSH)</term><term>Protein Transport (MeSH)</term><term>Proteins (chemistry)</term><term>Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Cytosol (métabolisme)</term><term>Humains (MeSH)</term><term>Membranes mitochondriales (métabolisme)</term><term>Oxydoréduction (MeSH)</term><term>Pliage des protéines (MeSH)</term><term>Protéines (composition chimique)</term><term>Protéines (métabolisme)</term><term>Transport des protéines (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Proteins</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Protéines</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cytosol</term><term>Mitochondrial Membranes</term><term>Proteins</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cytosol</term><term>Membranes mitochondriales</term><term>Protéines</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Humans</term><term>Oxidation-Reduction</term><term>Protein Folding</term><term>Protein Transport</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Humains</term><term>Oxydoréduction</term><term>Pliage des protéines</term><term>Transport des protéines</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Oxidative protein folding is confined to the bacterial periplasm, endoplasmic reticulum and the mitochondrial intermembrane space. Maintaining a redox balance requires the presence of reductive pathways. The major thiol-reducing pathways engage the thioredoxin and the glutaredoxin systems which are involved in removal of oxidants, protein proofreading and folding. Alterations in redox balance likely affect the flux of these redox pathways and are related to ageing and diseases such as neurodegenerative disorders and cancer. Here, we first review the well-studied oxidative and reductive processes in the bacterial periplasm and the endoplasmic reticulum, and then discuss the less understood process in the mitochondrial intermembrane space, highlighting its importance for the proper function of the cell.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">28746987</PMID><DateCompleted><Year>2017</Year><Month>10</Month><Day>04</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1873-3468</ISSN><JournalIssue CitedMedium="Internet"><Volume>591</Volume><Issue>17</Issue><PubDate><Year>2017</Year><Month>09</Month></PubDate></JournalIssue><Title>FEBS letters</Title><ISOAbbreviation>FEBS Lett</ISOAbbreviation></Journal><ArticleTitle>Cytosolic redox components regulate protein homeostasis via additional localisation in the mitochondrial intermembrane space.</ArticleTitle><Pagination><MedlinePgn>2661-2670</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1002/1873-3468.12766</ELocationID><Abstract><AbstractText>Oxidative protein folding is confined to the bacterial periplasm, endoplasmic reticulum and the mitochondrial intermembrane space. Maintaining a redox balance requires the presence of reductive pathways. The major thiol-reducing pathways engage the thioredoxin and the glutaredoxin systems which are involved in removal of oxidants, protein proofreading and folding. Alterations in redox balance likely affect the flux of these redox pathways and are related to ageing and diseases such as neurodegenerative disorders and cancer. Here, we first review the well-studied oxidative and reductive processes in the bacterial periplasm and the endoplasmic reticulum, and then discuss the less understood process in the mitochondrial intermembrane space, highlighting its importance for the proper function of the cell.</AbstractText><CopyrightInformation>© 2017 The Authors. FEBS Letters published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Cardenas-Rodriguez</LastName><ForeName>Mauricio</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Institute of Molecular, Cell and Systems Biology, College of Medical, Veterinary and Life Sciences, University of Glasgow, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Tokatlidis</LastName><ForeName>Kostas</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Institute of Molecular, Cell and Systems Biology, College of Medical, Veterinary and Life Sciences, University of Glasgow, UK.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><Agency>Wellcome Trust</Agency><Country>United Kingdom</Country></Grant><Grant><GrantID>202308/Z16/Z</GrantID><Agency>Wellcome Trust</Agency><Country>United 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