Yeast protein expression profile during acetic acid-induced apoptosis indicates causal involvement of the TOR pathway.
Identifieur interne : 001548 ( Main/Corpus ); précédent : 001547; suivant : 001549Yeast protein expression profile during acetic acid-induced apoptosis indicates causal involvement of the TOR pathway.
Auteurs : Bruno Almeida ; Steffen Ohlmeier ; Agostinho J. Almeida ; Frank Madeo ; Cecília Leão ; Fernando Rodrigues ; Paula LudovicoSource :
- Proteomics [ 1615-9861 ] ; 2009.
English descriptors
- KwdEn :
- Acetic Acid (pharmacology), Apoptosis (drug effects), Blotting, Western (MeSH), Electrophoresis, Gel, Two-Dimensional (MeSH), Gene Expression Regulation, Fungal (drug effects), Mass Spectrometry (MeSH), Protein-Serine-Threonine Kinases (metabolism), Reactive Oxygen Species (metabolism), Saccharomyces cerevisiae (drug effects), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (metabolism), Signal Transduction (drug effects).
- MESH :
- chemical , metabolism : Protein-Serine-Threonine Kinases, Reactive Oxygen Species, Saccharomyces cerevisiae Proteins.
- chemical , pharmacology : Acetic Acid.
- drug effects : Apoptosis, Gene Expression Regulation, Fungal, Saccharomyces cerevisiae, Signal Transduction.
- metabolism : Saccharomyces cerevisiae.
- Blotting, Western, Electrophoresis, Gel, Two-Dimensional, Mass Spectrometry.
Abstract
Although acetic acid has been shown to induce apoptosis in yeast, the exact apoptotic mechanisms remain unknown. Here, we studied the effects of acetic acid treatment on yeast cells by 2-DE, revealing alterations in the levels of proteins directly or indirectly linked with the target of rapamycin (TOR) pathway: amino-acid biosynthesis, transcription/translation machinery, carbohydrate metabolism, nucleotide biosynthesis, stress response, protein turnover and cell cycle. The increased levels of proteins involved in amino-acid biosynthesis presented a counteracting response to a severe intracellular amino-acid starvation induced by acetic acid. Deletion of GCN4 and GCN2 encoding key players of general amino-acid control (GAAC) system caused a higher resistance to acetic acid indicating an involvement of Gcn4p/Gcn2p in the apoptotic signaling. Involvement of the TOR pathway in acetic acid-induced apoptosis was also reflected by the higher survival rates associated to a terminal deoxynucleotidyl transferase-mediated dUTP nick end labeling (TUNEL)-negative phenotype and lower reactive oxygen species levels of Deltator1 cells. In addition, deletion mutants for several downstream mediators of the TOR pathway revealed that apoptotic signaling involves the phosphatases Pph21p and Pph22p but not Sit4p. Altogether, our results indicate that GAAC and TOR pathways (Tor1p) are involved in the signaling of acetic acid-induced apoptosis.
DOI: 10.1002/pmic.200700816
PubMed: 19137548
Links to Exploration step
pubmed:19137548Le document en format XML
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Almeida</name></author><author><name sortKey="Madeo, Frank" sort="Madeo, Frank" uniqKey="Madeo F" first="Frank" last="Madeo">Frank Madeo</name></author><author><name sortKey="Leao, Cecilia" sort="Leao, Cecilia" uniqKey="Leao C" first="Cecília" last="Leão">Cecília Leão</name></author><author><name sortKey="Rodrigues, Fernando" sort="Rodrigues, Fernando" uniqKey="Rodrigues F" first="Fernando" last="Rodrigues">Fernando Rodrigues</name></author><author><name sortKey="Ludovico, Paula" sort="Ludovico, Paula" uniqKey="Ludovico P" first="Paula" last="Ludovico">Paula Ludovico</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2009">2009</date><idno type="RBID">pubmed:19137548</idno><idno type="pmid">19137548</idno><idno type="doi">10.1002/pmic.200700816</idno><idno type="wicri:Area/Main/Corpus">001548</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">001548</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Yeast protein expression profile during acetic acid-induced apoptosis indicates causal involvement of the TOR pathway.</title><author><name sortKey="Almeida, Bruno" sort="Almeida, Bruno" uniqKey="Almeida B" first="Bruno" last="Almeida">Bruno Almeida</name><affiliation><nlm:affiliation>Life and Health Sciences Research Institute (ICVS), School of Health Sciences, University of Minho, Braga, Portugal.</nlm:affiliation></affiliation></author><author><name sortKey="Ohlmeier, Steffen" sort="Ohlmeier, Steffen" uniqKey="Ohlmeier S" first="Steffen" last="Ohlmeier">Steffen Ohlmeier</name></author><author><name sortKey="Almeida, Agostinho J" sort="Almeida, Agostinho J" uniqKey="Almeida A" first="Agostinho J" last="Almeida">Agostinho J. Almeida</name></author><author><name sortKey="Madeo, Frank" sort="Madeo, Frank" uniqKey="Madeo F" first="Frank" last="Madeo">Frank Madeo</name></author><author><name sortKey="Leao, Cecilia" sort="Leao, Cecilia" uniqKey="Leao C" first="Cecília" last="Leão">Cecília Leão</name></author><author><name sortKey="Rodrigues, Fernando" sort="Rodrigues, Fernando" uniqKey="Rodrigues F" first="Fernando" last="Rodrigues">Fernando Rodrigues</name></author><author><name sortKey="Ludovico, Paula" sort="Ludovico, Paula" uniqKey="Ludovico P" first="Paula" last="Ludovico">Paula Ludovico</name></author></analytic><series><title level="j">Proteomics</title><idno type="eISSN">1615-9861</idno><imprint><date when="2009" type="published">2009</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Acetic Acid (pharmacology)</term><term>Apoptosis (drug effects)</term><term>Blotting, Western (MeSH)</term><term>Electrophoresis, Gel, Two-Dimensional (MeSH)</term><term>Gene Expression Regulation, Fungal (drug effects)</term><term>Mass Spectrometry (MeSH)</term><term>Protein-Serine-Threonine Kinases (metabolism)</term><term>Reactive Oxygen Species (metabolism)</term><term>Saccharomyces cerevisiae (drug effects)</term><term>Saccharomyces cerevisiae (metabolism)</term><term>Saccharomyces cerevisiae Proteins (metabolism)</term><term>Signal Transduction (drug effects)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Protein-Serine-Threonine Kinases</term><term>Reactive Oxygen Species</term><term>Saccharomyces cerevisiae Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Acetic Acid</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Apoptosis</term><term>Gene Expression Regulation, Fungal</term><term>Saccharomyces cerevisiae</term><term>Signal Transduction</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Blotting, Western</term><term>Electrophoresis, Gel, Two-Dimensional</term><term>Mass Spectrometry</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Although acetic acid has been shown to induce apoptosis in yeast, the exact apoptotic mechanisms remain unknown. Here, we studied the effects of acetic acid treatment on yeast cells by 2-DE, revealing alterations in the levels of proteins directly or indirectly linked with the target of rapamycin (TOR) pathway: amino-acid biosynthesis, transcription/translation machinery, carbohydrate metabolism, nucleotide biosynthesis, stress response, protein turnover and cell cycle. The increased levels of proteins involved in amino-acid biosynthesis presented a counteracting response to a severe intracellular amino-acid starvation induced by acetic acid. Deletion of GCN4 and GCN2 encoding key players of general amino-acid control (GAAC) system caused a higher resistance to acetic acid indicating an involvement of Gcn4p/Gcn2p in the apoptotic signaling. Involvement of the TOR pathway in acetic acid-induced apoptosis was also reflected by the higher survival rates associated to a terminal deoxynucleotidyl transferase-mediated dUTP nick end labeling (TUNEL)-negative phenotype and lower reactive oxygen species levels of Deltator1 cells. In addition, deletion mutants for several downstream mediators of the TOR pathway revealed that apoptotic signaling involves the phosphatases Pph21p and Pph22p but not Sit4p. Altogether, our results indicate that GAAC and TOR pathways (Tor1p) are involved in the signaling of acetic acid-induced apoptosis.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">19137548</PMID><DateCompleted><Year>2009</Year><Month>05</Month><Day>05</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1615-9861</ISSN><JournalIssue CitedMedium="Internet"><Volume>9</Volume><Issue>3</Issue><PubDate><Year>2009</Year><Month>Feb</Month></PubDate></JournalIssue><Title>Proteomics</Title><ISOAbbreviation>Proteomics</ISOAbbreviation></Journal><ArticleTitle>Yeast protein expression profile during acetic acid-induced apoptosis indicates causal involvement of the TOR pathway.</ArticleTitle><Pagination><MedlinePgn>720-32</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1002/pmic.200700816</ELocationID><Abstract><AbstractText>Although acetic acid has been shown to induce apoptosis in yeast, the exact apoptotic mechanisms remain unknown. Here, we studied the effects of acetic acid treatment on yeast cells by 2-DE, revealing alterations in the levels of proteins directly or indirectly linked with the target of rapamycin (TOR) pathway: amino-acid biosynthesis, transcription/translation machinery, carbohydrate metabolism, nucleotide biosynthesis, stress response, protein turnover and cell cycle. The increased levels of proteins involved in amino-acid biosynthesis presented a counteracting response to a severe intracellular amino-acid starvation induced by acetic acid. Deletion of GCN4 and GCN2 encoding key players of general amino-acid control (GAAC) system caused a higher resistance to acetic acid indicating an involvement of Gcn4p/Gcn2p in the apoptotic signaling. Involvement of the TOR pathway in acetic acid-induced apoptosis was also reflected by the higher survival rates associated to a terminal deoxynucleotidyl transferase-mediated dUTP nick end labeling (TUNEL)-negative phenotype and lower reactive oxygen species levels of Deltator1 cells. In addition, deletion mutants for several downstream mediators of the TOR pathway revealed that apoptotic signaling involves the phosphatases Pph21p and Pph22p but not Sit4p. Altogether, our results indicate that GAAC and TOR pathways (Tor1p) are involved in the signaling of acetic acid-induced apoptosis.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Almeida</LastName><ForeName>Bruno</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Life and Health Sciences Research Institute (ICVS), School of Health Sciences, University of Minho, Braga, Portugal.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ohlmeier</LastName><ForeName>Steffen</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Almeida</LastName><ForeName>Agostinho J</ForeName><Initials>AJ</Initials></Author><Author ValidYN="Y"><LastName>Madeo</LastName><ForeName>Frank</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Leão</LastName><ForeName>Cecília</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Rodrigues</LastName><ForeName>Fernando</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Ludovico</LastName><ForeName>Paula</ForeName><Initials>P</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></Article><MedlineJournalInfo><Country>Germany</Country><MedlineTA>Proteomics</MedlineTA><NlmUniqueID>101092707</NlmUniqueID><ISSNLinking>1615-9853</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D017382">Reactive Oxygen Species</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029701">Saccharomyces cerevisiae Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber><NameOfSubstance UI="D017346">Protein-Serine-Threonine Kinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber><NameOfSubstance UI="C500749">target of rapamycin protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>Q40Q9N063P</RegistryNumber><NameOfSubstance UI="D019342">Acetic Acid</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D019342" MajorTopicYN="N">Acetic Acid</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017209" MajorTopicYN="N">Apoptosis</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015153" MajorTopicYN="N">Blotting, Western</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015180" MajorTopicYN="N">Electrophoresis, Gel, Two-Dimensional</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015966" MajorTopicYN="N">Gene Expression Regulation, Fungal</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013058" MajorTopicYN="N">Mass Spectrometry</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017346" MajorTopicYN="N">Protein-Serine-Threonine Kinases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017382" MajorTopicYN="N">Reactive Oxygen Species</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029701" MajorTopicYN="N">Saccharomyces cerevisiae Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015398" MajorTopicYN="N">Signal Transduction</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2009</Year><Month>1</Month><Day>13</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2009</Year><Month>1</Month><Day>13</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2009</Year><Month>5</Month><Day>6</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">19137548</ArticleId><ArticleId IdType="doi">10.1002/pmic.200700816</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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