Identification of potential protein dithiol-disulfide substrates of mammalian Grx2.
Identifieur interne : 000752 ( Main/Exploration ); précédent : 000751; suivant : 000753Identification of potential protein dithiol-disulfide substrates of mammalian Grx2.
Auteurs : Lena Dorothee Schütte [Allemagne] ; Stefan Baumeister ; Benjamin Weis ; Christoph Hudemann ; Eva-Maria Hanschmann ; Christopher Horst LilligSource :
- Biochimica et biophysica acta [ 0006-3002 ] ; 2013.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Cellules HeLa (MeSH), Cytosol (métabolisme), Cytosquelette (métabolisme), Disulfures (métabolisme), Glutarédoxines (métabolisme), Humains (MeSH), Isoformes de protéines (MeSH), Lignée cellulaire tumorale (MeSH), Mammifères (métabolisme), Motifs et domaines d'intéraction protéique (MeSH), Noyau de la cellule (métabolisme), Oxydoréduction (MeSH), Pliage des protéines (MeSH), Protéines (métabolisme), Souris (MeSH), Toluène (analogues et dérivés), Toluène (métabolisme).
- MESH :
- analogues et dérivés : Toluène.
- métabolisme : Cytosol, Cytosquelette, Disulfures, Glutarédoxines, Mammifères, Noyau de la cellule, Protéines, Toluène.
- Animaux, Cellules HeLa, Humains, Isoformes de protéines, Lignée cellulaire tumorale, Motifs et domaines d'intéraction protéique, Oxydoréduction, Pliage des protéines, Souris.
English descriptors
- KwdEn :
- Animals (MeSH), Cell Line, Tumor (MeSH), Cell Nucleus (metabolism), Cytoskeleton (metabolism), Cytosol (metabolism), Disulfides (metabolism), Glutaredoxins (metabolism), HeLa Cells (MeSH), Humans (MeSH), Mammals (metabolism), Mice (MeSH), Oxidation-Reduction (MeSH), Protein Folding (MeSH), Protein Interaction Domains and Motifs (MeSH), Protein Isoforms (MeSH), Proteins (metabolism), Toluene (analogs & derivatives), Toluene (metabolism).
- MESH :
- chemical , analogs & derivatives : Toluene.
- chemical , metabolism : Disulfides, Glutaredoxins, Proteins, Toluene.
- metabolism : Cell Nucleus, Cytoskeleton, Cytosol, Mammals.
- Animals, Cell Line, Tumor, HeLa Cells, Humans, Mice, Oxidation-Reduction, Protein Folding, Protein Interaction Domains and Motifs, Protein Isoforms.
Abstract
BACKGROUND
Glutaredoxins (Grxs) catalyze the reduction of protein disulfides via the dithiol mechanism and the de-/glutathionylation of substrates via the monothiol mechanism. These rapid, specific, and generally also reversible modifications are part of various signaling cascades regulating for instance cell proliferation, differentiation and apoptosis. Even though crucial functions of the conserved, mitochondrial Grx2a and the cytosolic/nuclear Grx2c isoforms have been proposed, only a few substrates have been identified in vitro or in vivo. The significance of redox signaling is emerging, yet a general lack of methods for the time-resolved analysis of these distinct and rapid modifications in vivo constitutes the biggest challenge in the redox signaling field.
METHODS AND RESULTS
Here, we have identified potential interaction partners for Grx2 isoforms in human HeLa cells and mouse tissues by an intermediate trapping approach. Some of the 50 potential substrates are part of the cytoskeleton or act in protein folding, cellular signaling and metabolism. Part of these interactions were further verified by immunoprecipitation or a newly established 2-D redox blot.
CONCLUSIONS
Our study demonstrates that Grx2 catalyzes both the specific oxidation and the reduction of cysteinyl residues in the same compartment at the same time and without affecting the global cellular thiol-redox state.
GENERAL SIGNIFICANCE
The knowledge of specific targets will be helpful in understanding the functions of Grx2. The 2-D redox blot may be useful for the analysis of the overall thiol-redox state of proteins with high molecular weight and numerous cysteinyl residues, that evaded analysis by previously described methods.
DOI: 10.1016/j.bbagen.2013.07.009
PubMed: 23872354
Affiliations:
Links toward previous steps (curation, corpus...)
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Baumeister</name></author><author><name sortKey="Weis, Benjamin" sort="Weis, Benjamin" uniqKey="Weis B" first="Benjamin" last="Weis">Benjamin Weis</name></author><author><name sortKey="Hudemann, Christoph" sort="Hudemann, Christoph" uniqKey="Hudemann C" first="Christoph" last="Hudemann">Christoph Hudemann</name></author><author><name sortKey="Hanschmann, Eva Maria" sort="Hanschmann, Eva Maria" uniqKey="Hanschmann E" first="Eva-Maria" last="Hanschmann">Eva-Maria Hanschmann</name></author><author><name sortKey="Lillig, Christopher Horst" sort="Lillig, Christopher Horst" uniqKey="Lillig C" first="Christopher Horst" last="Lillig">Christopher Horst Lillig</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2013">2013</date><idno type="RBID">pubmed:23872354</idno><idno type="pmid">23872354</idno><idno type="doi">10.1016/j.bbagen.2013.07.009</idno><idno type="wicri:Area/Main/Corpus">000723</idno><idno type="wicri:explorRef" wicri:stream="Main" 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Marburg</wicri:noRegion><wicri:noRegion>Philipps-University Marburg</wicri:noRegion></affiliation></author><author><name sortKey="Baumeister, Stefan" sort="Baumeister, Stefan" uniqKey="Baumeister S" first="Stefan" last="Baumeister">Stefan Baumeister</name></author><author><name sortKey="Weis, Benjamin" sort="Weis, Benjamin" uniqKey="Weis B" first="Benjamin" last="Weis">Benjamin Weis</name></author><author><name sortKey="Hudemann, Christoph" sort="Hudemann, Christoph" uniqKey="Hudemann C" first="Christoph" last="Hudemann">Christoph Hudemann</name></author><author><name sortKey="Hanschmann, Eva Maria" sort="Hanschmann, Eva Maria" uniqKey="Hanschmann E" first="Eva-Maria" last="Hanschmann">Eva-Maria Hanschmann</name></author><author><name sortKey="Lillig, Christopher Horst" sort="Lillig, Christopher Horst" uniqKey="Lillig C" first="Christopher Horst" last="Lillig">Christopher Horst Lillig</name></author></analytic><series><title level="j">Biochimica et biophysica acta</title><idno type="ISSN">0006-3002</idno><imprint><date when="2013" type="published">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term><term>Cell Line, Tumor (MeSH)</term><term>Cell Nucleus (metabolism)</term><term>Cytoskeleton (metabolism)</term><term>Cytosol (metabolism)</term><term>Disulfides (metabolism)</term><term>Glutaredoxins (metabolism)</term><term>HeLa Cells (MeSH)</term><term>Humans (MeSH)</term><term>Mammals (metabolism)</term><term>Mice (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Protein Folding (MeSH)</term><term>Protein Interaction Domains and Motifs (MeSH)</term><term>Protein Isoforms (MeSH)</term><term>Proteins (metabolism)</term><term>Toluene (analogs & derivatives)</term><term>Toluene (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Cellules HeLa (MeSH)</term><term>Cytosol (métabolisme)</term><term>Cytosquelette (métabolisme)</term><term>Disulfures (métabolisme)</term><term>Glutarédoxines (métabolisme)</term><term>Humains (MeSH)</term><term>Isoformes de protéines (MeSH)</term><term>Lignée cellulaire tumorale (MeSH)</term><term>Mammifères (métabolisme)</term><term>Motifs et domaines d'intéraction protéique (MeSH)</term><term>Noyau de la cellule (métabolisme)</term><term>Oxydoréduction (MeSH)</term><term>Pliage des protéines (MeSH)</term><term>Protéines (métabolisme)</term><term>Souris (MeSH)</term><term>Toluène (analogues et dérivés)</term><term>Toluène (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>Toluene</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Disulfides</term><term>Glutaredoxins</term><term>Proteins</term><term>Toluene</term></keywords><keywords scheme="MESH" qualifier="analogues et dérivés" xml:lang="fr"><term>Toluène</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cell Nucleus</term><term>Cytoskeleton</term><term>Cytosol</term><term>Mammals</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cytosol</term><term>Cytosquelette</term><term>Disulfures</term><term>Glutarédoxines</term><term>Mammifères</term><term>Noyau de la cellule</term><term>Protéines</term><term>Toluène</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cell Line, Tumor</term><term>HeLa Cells</term><term>Humans</term><term>Mice</term><term>Oxidation-Reduction</term><term>Protein Folding</term><term>Protein Interaction Domains and Motifs</term><term>Protein Isoforms</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Cellules HeLa</term><term>Humains</term><term>Isoformes de protéines</term><term>Lignée cellulaire tumorale</term><term>Motifs et domaines d'intéraction protéique</term><term>Oxydoréduction</term><term>Pliage des protéines</term><term>Souris</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p><b>BACKGROUND</b></p><p>Glutaredoxins (Grxs) catalyze the reduction of protein disulfides via the dithiol mechanism and the de-/glutathionylation of substrates via the monothiol mechanism. These rapid, specific, and generally also reversible modifications are part of various signaling cascades regulating for instance cell proliferation, differentiation and apoptosis. Even though crucial functions of the conserved, mitochondrial Grx2a and the cytosolic/nuclear Grx2c isoforms have been proposed, only a few substrates have been identified in vitro or in vivo. The significance of redox signaling is emerging, yet a general lack of methods for the time-resolved analysis of these distinct and rapid modifications in vivo constitutes the biggest challenge in the redox signaling field.</p></div><div type="abstract" xml:lang="en"><p><b>METHODS AND RESULTS</b></p><p>Here, we have identified potential interaction partners for Grx2 isoforms in human HeLa cells and mouse tissues by an intermediate trapping approach. Some of the 50 potential substrates are part of the cytoskeleton or act in protein folding, cellular signaling and metabolism. Part of these interactions were further verified by immunoprecipitation or a newly established 2-D redox blot.</p></div><div type="abstract" xml:lang="en"><p><b>CONCLUSIONS</b></p><p>Our study demonstrates that Grx2 catalyzes both the specific oxidation and the reduction of cysteinyl residues in the same compartment at the same time and without affecting the global cellular thiol-redox state.</p></div><div type="abstract" xml:lang="en"><p><b>GENERAL SIGNIFICANCE</b></p><p>The knowledge of specific targets will be helpful in understanding the functions of Grx2. The 2-D redox blot may be useful for the analysis of the overall thiol-redox state of proteins with high molecular weight and numerous cysteinyl residues, that evaded analysis by previously described methods.</p></div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">23872354</PMID><DateCompleted><Year>2014</Year><Month>03</Month><Day>21</Day></DateCompleted><DateRevised><Year>2016</Year><Month>11</Month><Day>26</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0006-3002</ISSN><JournalIssue CitedMedium="Print"><Volume>1830</Volume><Issue>11</Issue><PubDate><Year>2013</Year><Month>Nov</Month></PubDate></JournalIssue><Title>Biochimica et biophysica acta</Title><ISOAbbreviation>Biochim Biophys Acta</ISOAbbreviation></Journal><ArticleTitle>Identification of potential protein dithiol-disulfide substrates of mammalian Grx2.</ArticleTitle><Pagination><MedlinePgn>4999-5005</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.bbagen.2013.07.009</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0304-4165(13)00312-7</ELocationID><Abstract><AbstractText Label="BACKGROUND" NlmCategory="BACKGROUND">Glutaredoxins (Grxs) catalyze the reduction of protein disulfides via the dithiol mechanism and the de-/glutathionylation of substrates via the monothiol mechanism. These rapid, specific, and generally also reversible modifications are part of various signaling cascades regulating for instance cell proliferation, differentiation and apoptosis. Even though crucial functions of the conserved, mitochondrial Grx2a and the cytosolic/nuclear Grx2c isoforms have been proposed, only a few substrates have been identified in vitro or in vivo. The significance of redox signaling is emerging, yet a general lack of methods for the time-resolved analysis of these distinct and rapid modifications in vivo constitutes the biggest challenge in the redox signaling field.</AbstractText><AbstractText Label="METHODS AND RESULTS" NlmCategory="RESULTS">Here, we have identified potential interaction partners for Grx2 isoforms in human HeLa cells and mouse tissues by an intermediate trapping approach. Some of the 50 potential substrates are part of the cytoskeleton or act in protein folding, cellular signaling and metabolism. Part of these interactions were further verified by immunoprecipitation or a newly established 2-D redox blot.</AbstractText><AbstractText Label="CONCLUSIONS" NlmCategory="CONCLUSIONS">Our study demonstrates that Grx2 catalyzes both the specific oxidation and the reduction of cysteinyl residues in the same compartment at the same time and without affecting the global cellular thiol-redox state.</AbstractText><AbstractText Label="GENERAL SIGNIFICANCE" NlmCategory="CONCLUSIONS">The knowledge of specific targets will be helpful in understanding the functions of Grx2. The 2-D redox blot may be useful for the analysis of the overall thiol-redox state of proteins with high molecular weight and numerous cysteinyl residues, that evaded analysis by previously described methods.</AbstractText><CopyrightInformation>© 2013.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Schütte</LastName><ForeName>Lena Dorothee</ForeName><Initials>LD</Initials><AffiliationInfo><Affiliation>Institute for Clinical Cytobiology and Cytopathology, Philipps-University Marburg, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Baumeister</LastName><ForeName>Stefan</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Weis</LastName><ForeName>Benjamin</ForeName><Initials>B</Initials></Author><Author ValidYN="Y"><LastName>Hudemann</LastName><ForeName>Christoph</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Hanschmann</LastName><ForeName>Eva-Maria</ForeName><Initials>EM</Initials></Author><Author ValidYN="Y"><LastName>Lillig</LastName><ForeName>Christopher Horst</ForeName><Initials>CH</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2013</Year><Month>07</Month><Day>18</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Biochim Biophys Acta</MedlineTA><NlmUniqueID>0217513</NlmUniqueID><ISSNLinking>0006-3002</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004220">Disulfides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D020033">Protein Isoforms</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011506">Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>3FPU23BG52</RegistryNumber><NameOfSubstance UI="D014050">Toluene</NameOfSubstance></Chemical><Chemical><RegistryNumber>U89B11P7SC</RegistryNumber><NameOfSubstance UI="C004848">dithiol</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D045744" MajorTopicYN="N">Cell Line, Tumor</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002467" MajorTopicYN="N">Cell Nucleus</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName 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MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D051379" MajorTopicYN="N">Mice</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017510" MajorTopicYN="N">Protein Folding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054730" MajorTopicYN="N">Protein Interaction Domains and Motifs</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020033" MajorTopicYN="N">Protein Isoforms</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011506" MajorTopicYN="N">Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014050" MajorTopicYN="N">Toluene</DescriptorName><QualifierName UI="Q000031" MajorTopicYN="Y">analogs & derivatives</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Glutaredoxin</Keyword><Keyword MajorTopicYN="N">Intermediate trapping</Keyword><Keyword MajorTopicYN="N">Protein disulfide</Keyword><Keyword MajorTopicYN="N">Proteomics</Keyword><Keyword MajorTopicYN="N">Redox blot</Keyword><Keyword MajorTopicYN="N">Redox state</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2012</Year><Month>10</Month><Day>25</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2013</Year><Month>07</Month><Day>02</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2013</Year><Month>07</Month><Day>08</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2013</Year><Month>7</Month><Day>23</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2013</Year><Month>7</Month><Day>23</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2014</Year><Month>3</Month><Day>22</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">23872354</ArticleId><ArticleId IdType="pii">S0304-4165(13)00312-7</ArticleId><ArticleId IdType="doi">10.1016/j.bbagen.2013.07.009</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Allemagne</li></country></list><tree><noCountry><name sortKey="Baumeister, Stefan" sort="Baumeister, Stefan" uniqKey="Baumeister S" first="Stefan" last="Baumeister">Stefan Baumeister</name><name sortKey="Hanschmann, Eva Maria" sort="Hanschmann, Eva Maria" uniqKey="Hanschmann E" first="Eva-Maria" last="Hanschmann">Eva-Maria Hanschmann</name><name sortKey="Hudemann, Christoph" sort="Hudemann, Christoph" uniqKey="Hudemann C" first="Christoph" last="Hudemann">Christoph Hudemann</name><name sortKey="Lillig, Christopher Horst" sort="Lillig, Christopher Horst" uniqKey="Lillig C" first="Christopher Horst" last="Lillig">Christopher Horst Lillig</name><name sortKey="Weis, Benjamin" sort="Weis, Benjamin" uniqKey="Weis B" first="Benjamin" last="Weis">Benjamin Weis</name></noCountry><country name="Allemagne"><noRegion><name sortKey="Schutte, Lena Dorothee" sort="Schutte, Lena Dorothee" uniqKey="Schutte L" first="Lena Dorothee" last="Schütte">Lena Dorothee Schütte</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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