Copper-dependent interaction of glutaredoxin with the N termini of the copper-ATPases (ATP7A and ATP7B) defective in Menkes and Wilson diseases.
Identifieur interne : 000D60 ( Main/Exploration ); précédent : 000D59; suivant : 000D61Copper-dependent interaction of glutaredoxin with the N termini of the copper-ATPases (ATP7A and ATP7B) defective in Menkes and Wilson diseases.
Auteurs : Chris M. Lim [Australie] ; Michael A. Cater ; Julian F B. Mercer ; Sharon La FontaineSource :
- Biochemical and biophysical research communications [ 0006-291X ] ; 2006.
Descripteurs français
- KwdFr :
- MESH :
- métabolisme : Adenosine triphosphatases, Oxidoreductases, Transporteurs de cations.
- pharmacologie : Cuivre.
- Glutarédoxines, Humains, Motifs d'acides aminés, Séquence d'acides aminés, Techniques de double hybride.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Adenosine Triphosphatases, Cation Transport Proteins, Oxidoreductases.
- chemical , pharmacology : Copper.
- Amino Acid Motifs, Amino Acid Sequence, Copper-Transporting ATPases, Glutaredoxins, Humans, Two-Hybrid System Techniques.
Abstract
The P-type ATPases affected in Menkes and Wilson diseases, ATP7A and ATP7B, respectively, are key copper transporters that regulate copper homeostasis. The N termini of these proteins are critical in regulating their function and activity, and contain six copper-binding motifs MxCxxC. In this study, we describe the identification of glutaredoxin (GRX1) as an interacting partner of both ATP7A and ATP7B, confirmed by yeast two-hybrid technology and by co-immunoprecipitation from mammalian cells. The interaction required the presence of copper and intact metal-binding motifs. In addition, the interaction was related to the number of metal-binding domains available. GRX1 catalyses the reduction of disulphide bridges and reverses the glutathionylation of proteins to regulate and/or protect protein activity. We propose that GRX1 is essential for ATPase function and catalyses either the reduction of intramolecular disulphide bonds or the deglutathionylation of the cysteine residues within the CxxC motifs to facilitate copper-binding for subsequent transport.
DOI: 10.1016/j.bbrc.2006.07.067
PubMed: 16884690
Affiliations:
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Le document en format XML
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Cater</name></author><author><name sortKey="Mercer, Julian F B" sort="Mercer, Julian F B" uniqKey="Mercer J" first="Julian F B" last="Mercer">Julian F B. Mercer</name></author><author><name sortKey="La Fontaine, Sharon" sort="La Fontaine, Sharon" uniqKey="La Fontaine S" first="Sharon" last="La Fontaine">Sharon La Fontaine</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2006">2006</date><idno type="RBID">pubmed:16884690</idno><idno type="pmid">16884690</idno><idno type="doi">10.1016/j.bbrc.2006.07.067</idno><idno type="wicri:Area/Main/Corpus">000D31</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000D31</idno><idno type="wicri:Area/Main/Curation">000D31</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000D31</idno><idno type="wicri:Area/Main/Exploration">000D31</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Copper-dependent interaction of glutaredoxin with the N termini of the copper-ATPases (ATP7A and ATP7B) defective in Menkes and Wilson diseases.</title><author><name sortKey="Lim, Chris M" sort="Lim, Chris M" uniqKey="Lim C" first="Chris M" last="Lim">Chris M. 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Mercer</name></author><author><name sortKey="La Fontaine, Sharon" sort="La Fontaine, Sharon" uniqKey="La Fontaine S" first="Sharon" last="La Fontaine">Sharon La Fontaine</name></author></analytic><series><title level="j">Biochemical and biophysical research communications</title><idno type="ISSN">0006-291X</idno><imprint><date when="2006" type="published">2006</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Adenosine Triphosphatases (metabolism)</term><term>Amino Acid Motifs (MeSH)</term><term>Amino Acid Sequence (MeSH)</term><term>Cation Transport Proteins (metabolism)</term><term>Copper (pharmacology)</term><term>Copper-Transporting ATPases (MeSH)</term><term>Glutaredoxins (MeSH)</term><term>Humans (MeSH)</term><term>Oxidoreductases (metabolism)</term><term>Two-Hybrid System Techniques (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Adenosine triphosphatases (métabolisme)</term><term>Cuivre (pharmacologie)</term><term>Glutarédoxines (MeSH)</term><term>Humains (MeSH)</term><term>Motifs d'acides aminés (MeSH)</term><term>Oxidoreductases (métabolisme)</term><term>Séquence d'acides aminés (MeSH)</term><term>Techniques de double hybride (MeSH)</term><term>Transporteurs de cations (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Adenosine Triphosphatases</term><term>Cation Transport Proteins</term><term>Oxidoreductases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Copper</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Adenosine triphosphatases</term><term>Oxidoreductases</term><term>Transporteurs de cations</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Cuivre</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Motifs</term><term>Amino Acid Sequence</term><term>Copper-Transporting ATPases</term><term>Glutaredoxins</term><term>Humans</term><term>Two-Hybrid System Techniques</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Glutarédoxines</term><term>Humains</term><term>Motifs d'acides aminés</term><term>Séquence d'acides aminés</term><term>Techniques de double hybride</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The P-type ATPases affected in Menkes and Wilson diseases, ATP7A and ATP7B, respectively, are key copper transporters that regulate copper homeostasis. The N termini of these proteins are critical in regulating their function and activity, and contain six copper-binding motifs MxCxxC. In this study, we describe the identification of glutaredoxin (GRX1) as an interacting partner of both ATP7A and ATP7B, confirmed by yeast two-hybrid technology and by co-immunoprecipitation from mammalian cells. The interaction required the presence of copper and intact metal-binding motifs. In addition, the interaction was related to the number of metal-binding domains available. GRX1 catalyses the reduction of disulphide bridges and reverses the glutathionylation of proteins to regulate and/or protect protein activity. We propose that GRX1 is essential for ATPase function and catalyses either the reduction of intramolecular disulphide bonds or the deglutathionylation of the cysteine residues within the CxxC motifs to facilitate copper-binding for subsequent transport.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16884690</PMID><DateCompleted><Year>2006</Year><Month>10</Month><Day>10</Day></DateCompleted><DateRevised><Year>2019</Year><Month>12</Month><Day>10</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0006-291X</ISSN><JournalIssue CitedMedium="Print"><Volume>348</Volume><Issue>2</Issue><PubDate><Year>2006</Year><Month>Sep</Month><Day>22</Day></PubDate></JournalIssue><Title>Biochemical and biophysical research communications</Title><ISOAbbreviation>Biochem Biophys Res Commun</ISOAbbreviation></Journal><ArticleTitle>Copper-dependent interaction of glutaredoxin with the N termini of the copper-ATPases (ATP7A and ATP7B) defective in Menkes and Wilson diseases.</ArticleTitle><Pagination><MedlinePgn>428-36</MedlinePgn></Pagination><Abstract><AbstractText>The P-type ATPases affected in Menkes and Wilson diseases, ATP7A and ATP7B, respectively, are key copper transporters that regulate copper homeostasis. The N termini of these proteins are critical in regulating their function and activity, and contain six copper-binding motifs MxCxxC. In this study, we describe the identification of glutaredoxin (GRX1) as an interacting partner of both ATP7A and ATP7B, confirmed by yeast two-hybrid technology and by co-immunoprecipitation from mammalian cells. The interaction required the presence of copper and intact metal-binding motifs. In addition, the interaction was related to the number of metal-binding domains available. GRX1 catalyses the reduction of disulphide bridges and reverses the glutathionylation of proteins to regulate and/or protect protein activity. We propose that GRX1 is essential for ATPase function and catalyses either the reduction of intramolecular disulphide bonds or the deglutathionylation of the cysteine residues within the CxxC motifs to facilitate copper-binding for subsequent transport.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Lim</LastName><ForeName>Chris M</ForeName><Initials>CM</Initials><AffiliationInfo><Affiliation>Centre for Cellular and Molecular Biology, School of Life and Environmental Sciences, Deakin University, Burwood, Vic. 3125, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Cater</LastName><ForeName>Michael A</ForeName><Initials>MA</Initials></Author><Author ValidYN="Y"><LastName>Mercer</LastName><ForeName>Julian F B</ForeName><Initials>JF</Initials></Author><Author ValidYN="Y"><LastName>La Fontaine</LastName><ForeName>Sharon</ForeName><Initials>S</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>2006</Year><Month>07</Month><Day>24</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Biochem Biophys Res Commun</MedlineTA><NlmUniqueID>0372516</NlmUniqueID><ISSNLinking>0006-291X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D027682">Cation Transport Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>789U1901C5</RegistryNumber><NameOfSubstance UI="D003300">Copper</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.6.1.-</RegistryNumber><NameOfSubstance UI="D000251">Adenosine Triphosphatases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 7.2.2.8</RegistryNumber><NameOfSubstance UI="C081184">ATP7A protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 7.2.2.8</RegistryNumber><NameOfSubstance UI="C000612464">ATP7B protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 7.2.2.8</RegistryNumber><NameOfSubstance UI="D000073840">Copper-Transporting ATPases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000251" MajorTopicYN="N">Adenosine Triphosphatases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020816" MajorTopicYN="N">Amino Acid Motifs</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D027682" MajorTopicYN="N">Cation Transport Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003300" MajorTopicYN="N">Copper</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000073840" MajorTopicYN="N">Copper-Transporting ATPases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="N">Oxidoreductases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020798" MajorTopicYN="N">Two-Hybrid System Techniques</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2006</Year><Month>07</Month><Day>07</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2006</Year><Month>07</Month><Day>13</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2006</Year><Month>8</Month><Day>4</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2006</Year><Month>10</Month><Day>13</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2006</Year><Month>8</Month><Day>4</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">16884690</ArticleId><ArticleId IdType="pii">S0006-291X(06)01611-1</ArticleId><ArticleId IdType="doi">10.1016/j.bbrc.2006.07.067</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Australie</li></country></list><tree><noCountry><name sortKey="Cater, Michael A" sort="Cater, Michael A" uniqKey="Cater M" first="Michael A" last="Cater">Michael A. Cater</name><name sortKey="La Fontaine, Sharon" sort="La Fontaine, Sharon" uniqKey="La Fontaine S" first="Sharon" last="La Fontaine">Sharon La Fontaine</name><name sortKey="Mercer, Julian F B" sort="Mercer, Julian F B" uniqKey="Mercer J" first="Julian F B" last="Mercer">Julian F B. Mercer</name></noCountry><country name="Australie"><noRegion><name sortKey="Lim, Chris M" sort="Lim, Chris M" uniqKey="Lim C" first="Chris M" last="Lim">Chris M. Lim</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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