Heterologous expression of anti-apoptotic human 14-3-3β/α enhances iron-mediated programmed cell death in yeast.
Identifieur interne : 000827 ( Main/Exploration ); précédent : 000826; suivant : 000828Heterologous expression of anti-apoptotic human 14-3-3β/α enhances iron-mediated programmed cell death in yeast.
Auteurs : Rawan Eid [Canada] ; David R. Zhou [Canada] ; Nagla T T. Arab [Canada] ; Eric Boucher [Canada] ; Paul G. Young [Canada] ; Craig A. Mandato [Canada] ; Michael T. Greenwood [Canada]Source :
- PloS one [ 1932-6203 ] ; 2017.
Descripteurs français
- KwdFr :
- Cuivre (métabolisme), Cuivre (toxicité), Expression des gènes (MeSH), Fer (métabolisme), Fer (toxicité), Ferritines (génétique), Ferritines (métabolisme), Humains (MeSH), Mutation (MeSH), Protéines 14-3-3 (génétique), Protéines 14-3-3 (métabolisme), Saccharomyces cerevisiae (cytologie), Saccharomyces cerevisiae (génétique), Saccharomyces cerevisiae (métabolisme).
- MESH :
- cytologie : Saccharomyces cerevisiae.
- génétique : Ferritines, Protéines 14-3-3, Saccharomyces cerevisiae.
- métabolisme : Cuivre, Fer, Ferritines, Protéines 14-3-3, Saccharomyces cerevisiae.
- toxicité : Cuivre, Fer.
- Expression des gènes, Humains, Mutation.
English descriptors
- KwdEn :
- 14-3-3 Proteins (genetics), 14-3-3 Proteins (metabolism), Copper (metabolism), Copper (toxicity), Ferritins (genetics), Ferritins (metabolism), Gene Expression (MeSH), Humans (MeSH), Iron (metabolism), Iron (toxicity), Mutation (MeSH), Saccharomyces cerevisiae (cytology), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (metabolism).
- MESH :
- chemical , genetics : 14-3-3 Proteins, Ferritins.
- chemical , metabolism : 14-3-3 Proteins, Copper, Ferritins, Iron.
- chemical , toxicity : Copper, Iron.
- cytology : Saccharomyces cerevisiae.
- genetics : Saccharomyces cerevisiae.
- metabolism : Saccharomyces cerevisiae.
- Gene Expression, Humans, Mutation.
Abstract
The induction of Programmed Cell Death (PCD) requires the activation of complex responses involving the interplay of a variety of different cellular proteins, pathways, and processes. Uncovering the mechanisms regulating PCD requires an understanding of the different processes that both positively and negatively regulate cell death. Here we have examined the response of normal as well as PCD resistant yeast cells to different PCD inducing stresses. As expected cells expressing the pro-survival human 14-3-3β/α sequence show increased resistance to numerous stresses including copper and rapamycin. In contrast, other stresses including iron were more lethal in PCD resistant 14-3-3β/α expressing cells. The increased sensitivity to PCD was not iron and 14-3-3β/α specific since it was also observed with other stresses (hydroxyurea and zinc) and other pro-survival sequences (human TC-1 and H-ferritin). Although microscopical examination revealed little differences in morphology with iron or copper stresses, cells undergoing PCD in response to high levels of prolonged copper treatment were reduced in size. This supports the interaction some forms of PCD have with the mechanisms regulating cell growth. Analysis of iron-mediated effects in yeast mutant strains lacking key regulators suggests that a functional vacuole is required to mediate the synergistic effects of iron and 14-3-3β/α on yeast PCD. Finally, mild sub-lethal levels of copper were found to attenuate the observed inhibitory effects of iron. Taken together, we propose a model in which a subset of stresses like iron induces a complex process that requires the cross-talk of two different PCD inducing pathways.
DOI: 10.1371/journal.pone.0184151
PubMed: 28854230
PubMed Central: PMC5576682
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Zhou</name><affiliation wicri:level="4"><nlm:affiliation>Department of Anatomy and Cell Biology, McGill University, Montreal, Quebec, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Department of Anatomy and Cell Biology, McGill University, Montreal, Quebec</wicri:regionArea><orgName type="university">Université McGill</orgName><placeName><settlement type="city">Montréal</settlement><region type="state">Québec</region></placeName></affiliation></author><author><name sortKey="Arab, Nagla T T" sort="Arab, Nagla T T" uniqKey="Arab N" first="Nagla T T" last="Arab">Nagla T T. Arab</name><affiliation wicri:level="1"><nlm:affiliation>Department of Chemistry and Chemical Engineering, Royal Military College, Kingston, Ontario, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Department of Chemistry and Chemical Engineering, Royal Military College, Kingston, Ontario</wicri:regionArea><wicri:noRegion>Ontario</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:affiliation>Department of Biology, Queen's University, Kingston, Ontario, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Department of Biology, Queen's University, Kingston, Ontario</wicri:regionArea><wicri:noRegion>Ontario</wicri:noRegion></affiliation></author><author><name sortKey="Boucher, Eric" sort="Boucher, Eric" uniqKey="Boucher E" first="Eric" last="Boucher">Eric Boucher</name><affiliation wicri:level="4"><nlm:affiliation>Department of Anatomy and Cell Biology, McGill University, Montreal, Quebec, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Department of Anatomy and Cell Biology, McGill University, Montreal, Quebec</wicri:regionArea><orgName type="university">Université McGill</orgName><placeName><settlement type="city">Montréal</settlement><region type="state">Québec</region></placeName></affiliation></author><author><name sortKey="Young, Paul G" sort="Young, Paul G" uniqKey="Young P" first="Paul G" last="Young">Paul G. Young</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biology, Queen's University, Kingston, Ontario, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Department of Biology, Queen's University, Kingston, Ontario</wicri:regionArea><wicri:noRegion>Ontario</wicri:noRegion></affiliation></author><author><name sortKey="Mandato, Craig A" sort="Mandato, Craig A" uniqKey="Mandato C" first="Craig A" last="Mandato">Craig A. Mandato</name><affiliation wicri:level="4"><nlm:affiliation>Department of Anatomy and Cell Biology, McGill University, Montreal, Quebec, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Department of Anatomy and Cell Biology, McGill University, Montreal, Quebec</wicri:regionArea><orgName type="university">Université McGill</orgName><placeName><settlement type="city">Montréal</settlement><region type="state">Québec</region></placeName></affiliation></author><author><name sortKey="Greenwood, Michael T" sort="Greenwood, Michael T" uniqKey="Greenwood M" first="Michael T" last="Greenwood">Michael T. Greenwood</name><affiliation wicri:level="1"><nlm:affiliation>Department of Chemistry and Chemical Engineering, Royal Military College, Kingston, Ontario, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Department of Chemistry and Chemical Engineering, Royal Military College, Kingston, Ontario</wicri:regionArea><wicri:noRegion>Ontario</wicri:noRegion></affiliation></author></analytic><series><title level="j">PloS one</title><idno type="eISSN">1932-6203</idno><imprint><date when="2017" type="published">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>14-3-3 Proteins (genetics)</term><term>14-3-3 Proteins (metabolism)</term><term>Copper (metabolism)</term><term>Copper (toxicity)</term><term>Ferritins (genetics)</term><term>Ferritins (metabolism)</term><term>Gene Expression (MeSH)</term><term>Humans (MeSH)</term><term>Iron (metabolism)</term><term>Iron (toxicity)</term><term>Mutation (MeSH)</term><term>Saccharomyces cerevisiae (cytology)</term><term>Saccharomyces cerevisiae (genetics)</term><term>Saccharomyces cerevisiae (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Cuivre (métabolisme)</term><term>Cuivre (toxicité)</term><term>Expression des gènes (MeSH)</term><term>Fer (métabolisme)</term><term>Fer (toxicité)</term><term>Ferritines (génétique)</term><term>Ferritines (métabolisme)</term><term>Humains (MeSH)</term><term>Mutation (MeSH)</term><term>Protéines 14-3-3 (génétique)</term><term>Protéines 14-3-3 (métabolisme)</term><term>Saccharomyces cerevisiae (cytologie)</term><term>Saccharomyces cerevisiae (génétique)</term><term>Saccharomyces cerevisiae (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>14-3-3 Proteins</term><term>Ferritins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>14-3-3 Proteins</term><term>Copper</term><term>Ferritins</term><term>Iron</term></keywords><keywords scheme="MESH" type="chemical" qualifier="toxicity" xml:lang="en"><term>Copper</term><term>Iron</term></keywords><keywords scheme="MESH" qualifier="cytologie" xml:lang="fr"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="cytology" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Ferritines</term><term>Protéines 14-3-3</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cuivre</term><term>Fer</term><term>Ferritines</term><term>Protéines 14-3-3</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="toxicité" xml:lang="fr"><term>Cuivre</term><term>Fer</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Gene Expression</term><term>Humans</term><term>Mutation</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Expression des gènes</term><term>Humains</term><term>Mutation</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The induction of Programmed Cell Death (PCD) requires the activation of complex responses involving the interplay of a variety of different cellular proteins, pathways, and processes. Uncovering the mechanisms regulating PCD requires an understanding of the different processes that both positively and negatively regulate cell death. Here we have examined the response of normal as well as PCD resistant yeast cells to different PCD inducing stresses. As expected cells expressing the pro-survival human 14-3-3β/α sequence show increased resistance to numerous stresses including copper and rapamycin. In contrast, other stresses including iron were more lethal in PCD resistant 14-3-3β/α expressing cells. The increased sensitivity to PCD was not iron and 14-3-3β/α specific since it was also observed with other stresses (hydroxyurea and zinc) and other pro-survival sequences (human TC-1 and H-ferritin). Although microscopical examination revealed little differences in morphology with iron or copper stresses, cells undergoing PCD in response to high levels of prolonged copper treatment were reduced in size. This supports the interaction some forms of PCD have with the mechanisms regulating cell growth. Analysis of iron-mediated effects in yeast mutant strains lacking key regulators suggests that a functional vacuole is required to mediate the synergistic effects of iron and 14-3-3β/α on yeast PCD. Finally, mild sub-lethal levels of copper were found to attenuate the observed inhibitory effects of iron. Taken together, we propose a model in which a subset of stresses like iron induces a complex process that requires the cross-talk of two different PCD inducing pathways.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">28854230</PMID><DateCompleted><Year>2017</Year><Month>10</Month><Day>16</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Electronic-eCollection"><Journal><ISSN IssnType="Electronic">1932-6203</ISSN><JournalIssue CitedMedium="Internet"><Volume>12</Volume><Issue>8</Issue><PubDate><Year>2017</Year></PubDate></JournalIssue><Title>PloS one</Title><ISOAbbreviation>PLoS One</ISOAbbreviation></Journal><ArticleTitle>Heterologous expression of anti-apoptotic human 14-3-3β/α enhances iron-mediated programmed cell death in yeast.</ArticleTitle><Pagination><MedlinePgn>e0184151</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1371/journal.pone.0184151</ELocationID><Abstract><AbstractText>The induction of Programmed Cell Death (PCD) requires the activation of complex responses involving the interplay of a variety of different cellular proteins, pathways, and processes. Uncovering the mechanisms regulating PCD requires an understanding of the different processes that both positively and negatively regulate cell death. Here we have examined the response of normal as well as PCD resistant yeast cells to different PCD inducing stresses. As expected cells expressing the pro-survival human 14-3-3β/α sequence show increased resistance to numerous stresses including copper and rapamycin. In contrast, other stresses including iron were more lethal in PCD resistant 14-3-3β/α expressing cells. The increased sensitivity to PCD was not iron and 14-3-3β/α specific since it was also observed with other stresses (hydroxyurea and zinc) and other pro-survival sequences (human TC-1 and H-ferritin). Although microscopical examination revealed little differences in morphology with iron or copper stresses, cells undergoing PCD in response to high levels of prolonged copper treatment were reduced in size. This supports the interaction some forms of PCD have with the mechanisms regulating cell growth. Analysis of iron-mediated effects in yeast mutant strains lacking key regulators suggests that a functional vacuole is required to mediate the synergistic effects of iron and 14-3-3β/α on yeast PCD. Finally, mild sub-lethal levels of copper were found to attenuate the observed inhibitory effects of iron. Taken together, we propose a model in which a subset of stresses like iron induces a complex process that requires the cross-talk of two different PCD inducing pathways.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Eid</LastName><ForeName>Rawan</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Department of Chemistry and Chemical Engineering, Royal Military College, Kingston, Ontario, Canada.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Biology, Queen's University, Kingston, Ontario, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Zhou</LastName><ForeName>David R</ForeName><Initials>DR</Initials><AffiliationInfo><Affiliation>Department of Anatomy and Cell Biology, McGill University, Montreal, Quebec, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Arab</LastName><ForeName>Nagla T T</ForeName><Initials>NTT</Initials><AffiliationInfo><Affiliation>Department of Chemistry and Chemical Engineering, Royal Military College, Kingston, Ontario, Canada.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Biology, Queen's University, Kingston, Ontario, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Boucher</LastName><ForeName>Eric</ForeName><Initials>E</Initials><AffiliationInfo><Affiliation>Department of Anatomy and Cell Biology, McGill University, Montreal, Quebec, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Young</LastName><ForeName>Paul G</ForeName><Initials>PG</Initials><AffiliationInfo><Affiliation>Department of Biology, Queen's University, Kingston, Ontario, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mandato</LastName><ForeName>Craig A</ForeName><Initials>CA</Initials><AffiliationInfo><Affiliation>Department of Anatomy and Cell Biology, McGill University, Montreal, Quebec, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Greenwood</LastName><ForeName>Michael T</ForeName><Initials>MT</Initials><Identifier Source="ORCID">http://orcid.org/0000-0003-0890-3434</Identifier><AffiliationInfo><Affiliation>Department of Chemistry and Chemical Engineering, Royal Military College, Kingston, Ontario, Canada.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2017</Year><Month>08</Month><Day>30</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>PLoS One</MedlineTA><NlmUniqueID>101285081</NlmUniqueID><ISSNLinking>1932-6203</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D048948">14-3-3 Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C482982">YWHAB protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>789U1901C5</RegistryNumber><NameOfSubstance UI="D003300">Copper</NameOfSubstance></Chemical><Chemical><RegistryNumber>9007-73-2</RegistryNumber><NameOfSubstance UI="D005293">Ferritins</NameOfSubstance></Chemical><Chemical><RegistryNumber>E1UOL152H7</RegistryNumber><NameOfSubstance UI="D007501">Iron</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D048948" MajorTopicYN="N">14-3-3 Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003300" MajorTopicYN="N">Copper</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000633" MajorTopicYN="N">toxicity</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005293" MajorTopicYN="N">Ferritins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015870" MajorTopicYN="N">Gene Expression</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007501" MajorTopicYN="N">Iron</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000633" MajorTopicYN="N">toxicity</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000166" MajorTopicYN="Y">cytology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2017</Year><Month>06</Month><Day>24</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2017</Year><Month>08</Month><Day>20</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2017</Year><Month>8</Month><Day>31</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2017</Year><Month>8</Month><Day>31</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2017</Year><Month>10</Month><Day>17</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>epublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">28854230</ArticleId><ArticleId 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