GlutaredoxinV1, Main, Exploration, bibRecord, 000317

Redox regulation of the yeast voltage-gated Ca2+ channel homolog Cch1p by glutathionylation of specific cysteine residues.

Identifieur interne : 000317 ( Main/Exploration ); précédent : 000316; suivant : 000318

Redox regulation of the yeast voltage-gated Ca2+ channel homolog Cch1p by glutathionylation of specific cysteine residues.

Auteurs : Avinash Chandel [Inde] ; Anand K. Bachhawat [Inde]

Source :

Journal of cell science [ 1477-9137 ] ; 2017.

RBID : pubmed:28576969

Descripteurs français

English descriptors

KwdEn :
- Alanine (genetics), Amino Acid Sequence (MeSH), Calcium Channels (genetics), Calcium Channels (metabolism), Conserved Sequence (MeSH), Cysteine (genetics), Cysteine (metabolism), Cytoplasm (metabolism), Glutathione (metabolism), Hydrogen-Ion Concentration (MeSH), Mutation (MeSH), Oxidation-Reduction (MeSH), Oxidative Stress (physiology), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism), Thioredoxins (metabolism).
MESH :
- chemical , genetics : Alanine, Calcium Channels, Cysteine, Saccharomyces cerevisiae Proteins.
- chemical , metabolism : Calcium Channels, Cysteine, Glutathione, Saccharomyces cerevisiae Proteins, Thioredoxins.
- genetics : Saccharomyces cerevisiae.
- metabolism : Cytoplasm, Saccharomyces cerevisiae.
- physiology : Oxidative Stress.
- Amino Acid Sequence, Conserved Sequence, Hydrogen-Ion Concentration, Mutation, Oxidation-Reduction.

Abstract

Cch1p, the yeast homolog of the pore-forming subunit α₁ of the mammalian voltage-gated Ca²⁺ channel (VGCC), is located on the plasma membrane and mediates the redox-dependent influx of Ca²⁺ Cch1p is known to undergo both rapid activation (after oxidative stress and or a change to high pH) and slow activation (after ER stress and mating pheromone activation), but the mechanism of activation is not known. We demonstrate here that both the fast activation (exposure to pH 8-8.5 or treatment with H₂O₂) and the slow activation (treatment with tunicamycin or α-factor) are mediated through a common redox-dependent mechanism. Furthermore, through mutational analysis of all 18 exposed cysteine residues in the Cch1p protein, we show that the four mutants C587A, C606A, C636A and C642A, which are clustered together in a common cytoplasmic loop region, were functionally defective for both fast and slow activations, and also showed reduced glutathionylation. These four cysteine residues are also conserved across phyla, suggesting a conserved mechanism of activation. Investigations into the enzymes involved in the activation reveal that the yeast glutathione S-transferase Gtt1p is involved in the glutathionylation of Cch1p, while the thioredoxin Trx2p plays a role in the Cch1p deglutathionylation.

DOI: 10.1242/jcs.202853
PubMed: 28576969

Affiliations:

Inde

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Le document en format XML

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 channel homolog Cch1p by glutathionylation of specific cysteine residues.</title>
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<sourceDesc><biblStruct><analytic><title xml:lang="en">Redox regulation of the yeast voltage-gated Ca<sup>2+</sup>
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<author><name sortKey="Bachhawat, Anand K" sort="Bachhawat, Anand K" uniqKey="Bachhawat A" first="Anand K" last="Bachhawat">Anand K. Bachhawat</name>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Alanine (genetics)</term>
<term>Amino Acid Sequence (MeSH)</term>
<term>Calcium Channels (genetics)</term>
<term>Calcium Channels (metabolism)</term>
<term>Conserved Sequence (MeSH)</term>
<term>Cysteine (genetics)</term>
<term>Cysteine (metabolism)</term>
<term>Cytoplasm (metabolism)</term>
<term>Glutathione (metabolism)</term>
<term>Hydrogen-Ion Concentration (MeSH)</term>
<term>Mutation (MeSH)</term>
<term>Oxidation-Reduction (MeSH)</term>
<term>Oxidative Stress (physiology)</term>
<term>Saccharomyces cerevisiae (genetics)</term>
<term>Saccharomyces cerevisiae (metabolism)</term>
<term>Saccharomyces cerevisiae Proteins (genetics)</term>
<term>Saccharomyces cerevisiae Proteins (metabolism)</term>
<term>Thioredoxins (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Alanine (génétique)</term>
<term>Canaux calciques (génétique)</term>
<term>Canaux calciques (métabolisme)</term>
<term>Concentration en ions d'hydrogène (MeSH)</term>
<term>Cystéine (génétique)</term>
<term>Cystéine (métabolisme)</term>
<term>Cytoplasme (métabolisme)</term>
<term>Glutathion (métabolisme)</term>
<term>Mutation (MeSH)</term>
<term>Oxydoréduction (MeSH)</term>
<term>Protéines de Saccharomyces cerevisiae (génétique)</term>
<term>Protéines de Saccharomyces cerevisiae (métabolisme)</term>
<term>Saccharomyces cerevisiae (génétique)</term>
<term>Saccharomyces cerevisiae (métabolisme)</term>
<term>Stress oxydatif (physiologie)</term>
<term>Séquence conservée (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
<term>Thiorédoxines (métabolisme)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Alanine</term>
<term>Calcium Channels</term>
<term>Cysteine</term>
<term>Saccharomyces cerevisiae Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Calcium Channels</term>
<term>Cysteine</term>
<term>Glutathione</term>
<term>Saccharomyces cerevisiae Proteins</term>
<term>Thioredoxins</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Alanine</term>
<term>Canaux calciques</term>
<term>Cystéine</term>
<term>Protéines de Saccharomyces cerevisiae</term>
<term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cytoplasm</term>
<term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Canaux calciques</term>
<term>Cystéine</term>
<term>Cytoplasme</term>
<term>Glutathion</term>
<term>Protéines de Saccharomyces cerevisiae</term>
<term>Saccharomyces cerevisiae</term>
<term>Thiorédoxines</term>
</keywords>
<keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Stress oxydatif</term>
</keywords>
<keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Oxidative Stress</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Conserved Sequence</term>
<term>Hydrogen-Ion Concentration</term>
<term>Mutation</term>
<term>Oxidation-Reduction</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Concentration en ions d'hydrogène</term>
<term>Mutation</term>
<term>Oxydoréduction</term>
<term>Séquence conservée</term>
<term>Séquence d'acides aminés</term>
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<front><div type="abstract" xml:lang="en">Cch1p, the yeast homolog of the pore-forming subunit α<sub>1</sub>
 of the mammalian voltage-gated Ca<sup>2+</sup>
 channel (VGCC), is located on the plasma membrane and mediates the redox-dependent influx of Ca<sup>2+</sup>
 Cch1p is known to undergo both rapid activation (after oxidative stress and or a change to high pH) and slow activation (after ER stress and mating pheromone activation), but the mechanism of activation is not known. We demonstrate here that both the fast activation (exposure to pH 8-8.5 or treatment with H<sub>2</sub>
O<sub>2</sub>
) and the slow activation (treatment with tunicamycin or α-factor) are mediated through a common redox-dependent mechanism. Furthermore, through mutational analysis of all 18 exposed cysteine residues in the Cch1p protein, we show that the four mutants C587A, C606A, C636A and C642A, which are clustered together in a common cytoplasmic loop region, were functionally defective for both fast and slow activations, and also showed reduced glutathionylation. These four cysteine residues are also conserved across phyla, suggesting a conserved mechanism of activation. Investigations into the enzymes involved in the activation reveal that the yeast glutathione S-transferase Gtt1p is involved in the glutathionylation of Cch1p, while the thioredoxin Trx2p plays a role in the Cch1p deglutathionylation.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">28576969</PMID>
<DateCompleted><Year>2018</Year>
<Month>09</Month>
<Day>11</Day>
</DateCompleted>
<DateRevised><Year>2018</Year>
<Month>09</Month>
<Day>11</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1477-9137</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>130</Volume>
<Issue>14</Issue>
<PubDate><Year>2017</Year>
<Month>Jul</Month>
<Day>15</Day>
</PubDate>
</JournalIssue>
<Title>Journal of cell science</Title>
<ISOAbbreviation>J Cell Sci</ISOAbbreviation>
</Journal>
<ArticleTitle>Redox regulation of the yeast voltage-gated Ca<sup>2+</sup>
 channel homolog Cch1p by glutathionylation of specific cysteine residues.</ArticleTitle>
<Pagination><MedlinePgn>2317-2328</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1242/jcs.202853</ELocationID>
<Abstract><AbstractText>Cch1p, the yeast homolog of the pore-forming subunit α<sub>1</sub>
 of the mammalian voltage-gated Ca<sup>2+</sup>
 channel (VGCC), is located on the plasma membrane and mediates the redox-dependent influx of Ca<sup>2+</sup>
 Cch1p is known to undergo both rapid activation (after oxidative stress and or a change to high pH) and slow activation (after ER stress and mating pheromone activation), but the mechanism of activation is not known. We demonstrate here that both the fast activation (exposure to pH 8-8.5 or treatment with H<sub>2</sub>
O<sub>2</sub>
) and the slow activation (treatment with tunicamycin or α-factor) are mediated through a common redox-dependent mechanism. Furthermore, through mutational analysis of all 18 exposed cysteine residues in the Cch1p protein, we show that the four mutants C587A, C606A, C636A and C642A, which are clustered together in a common cytoplasmic loop region, were functionally defective for both fast and slow activations, and also showed reduced glutathionylation. These four cysteine residues are also conserved across phyla, suggesting a conserved mechanism of activation. Investigations into the enzymes involved in the activation reveal that the yeast glutathione S-transferase Gtt1p is involved in the glutathionylation of Cch1p, while the thioredoxin Trx2p plays a role in the Cch1p deglutathionylation.</AbstractText>
<CopyrightInformation>© 2017. Published by The Company of Biologists Ltd.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Chandel</LastName>
<ForeName>Avinash</ForeName>
<Initials>A</Initials>
<AffiliationInfo><Affiliation>Department of Biological Sciences, Indian Institute of Science Education & Research (IISER), Sector 81, Mohali, Punjab 140306, India.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Bachhawat</LastName>
<ForeName>Anand K</ForeName>
<Initials>AK</Initials>
<Identifier Source="ORCID">http://orcid.org/0000-0003-1529-3769</Identifier>
<AffiliationInfo><Affiliation>Department of Biological Sciences, Indian Institute of Science Education & Research (IISER), Sector 81, Mohali, Punjab 140306, India anand@iisermohali.ac.in.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2017</Year>
<Month>06</Month>
<Day>02</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>England</Country>
<MedlineTA>J Cell Sci</MedlineTA>
<NlmUniqueID>0052457</NlmUniqueID>
<ISSNLinking>0021-9533</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="C108765">CCH1 protein, S cerevisiae</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D015220">Calcium Channels</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D029701">Saccharomyces cerevisiae Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="C516110">TRX2 protein, S cerevisiae</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>52500-60-4</RegistryNumber>
<NameOfSubstance UI="D013879">Thioredoxins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber>
<NameOfSubstance UI="D005978">Glutathione</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>K848JZ4886</RegistryNumber>
<NameOfSubstance UI="D003545">Cysteine</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>OF5P57N2ZX</RegistryNumber>
<NameOfSubstance UI="D000409">Alanine</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<CommentsCorrectionsList><CommentsCorrections RefType="ErratumIn"><RefSource>J Cell Sci. 2019 Sep 20;132(18):</RefSource>
<PMID Version="1">31540946</PMID>
</CommentsCorrections>
</CommentsCorrectionsList>
<MeshHeadingList><MeshHeading><DescriptorName UI="D000409" MajorTopicYN="N">Alanine</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D015220" MajorTopicYN="N">Calcium Channels</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D017124" MajorTopicYN="N">Conserved Sequence</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D003545" MajorTopicYN="N">Cysteine</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D003593" MajorTopicYN="N">Cytoplasm</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006863" MajorTopicYN="N">Hydrogen-Ion Concentration</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D018384" MajorTopicYN="N">Oxidative Stress</DescriptorName>
<QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D029701" MajorTopicYN="N">Saccharomyces cerevisiae Proteins</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
</MeshHeadingList>
<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Glutaredoxins</Keyword>
<Keyword MajorTopicYN="N">Glutathione S-transferase</Keyword>
<Keyword MajorTopicYN="N">Redox</Keyword>
<Keyword MajorTopicYN="N">Thioredoxins</Keyword>
<Keyword MajorTopicYN="N">Voltage-gated Ca2+ channels</Keyword>
</KeywordList>
<CoiStatement>Competing interestsThe authors declare no competing or financial interests.</CoiStatement>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="received"><Year>2017</Year>
<Month>02</Month>
<Day>20</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="accepted"><Year>2017</Year>
<Month>05</Month>
<Day>26</Day>
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<Month>6</Month>
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<ArticleIdList><ArticleId IdType="pubmed">28576969</ArticleId>
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<ArticleId IdType="doi">10.1242/jcs.202853</ArticleId>
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<affiliations><list><country><li>Inde</li>
</country>
</list>
<tree><country name="Inde"><noRegion><name sortKey="Chandel, Avinash" sort="Chandel, Avinash" uniqKey="Chandel A" first="Avinash" last="Chandel">Avinash Chandel</name>
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Redox regulation of the yeast voltage-gated Ca2+ channel homolog Cch1p by glutathionylation of specific cysteine residues.

Redox regulation of the yeast voltage-gated Ca2+ channel homolog Cch1p by glutathionylation of specific cysteine residues.

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Abstract

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