Yeast endosulfines control entry into quiescence and chronological life span by inhibiting protein phosphatase 2A.
Identifieur interne : 000F48 ( Main/Exploration ); précédent : 000F47; suivant : 000F49Yeast endosulfines control entry into quiescence and chronological life span by inhibiting protein phosphatase 2A.
Auteurs : Séverine Bontron [Suisse] ; Malika Jaquenoud ; Stefania Vaga ; Nicolas Talarek ; Bernd Bodenmiller ; Ruedi Aebersold ; Claudio De VirgilioSource :
- Cell reports [ 2211-1247 ] ; 2013.
Descripteurs français
- KwdFr :
- Coloration et marquage (MeSH), Données de séquences moléculaires (MeSH), Liaison aux protéines (effets des médicaments et des substances chimiques), Peptides (métabolisme), Phosphorylation (effets des médicaments et des substances chimiques), Protein Phosphatase 2 (antagonistes et inhibiteurs), Protein Phosphatase 2 (métabolisme), Protéines de Saccharomyces cerevisiae (composition chimique), Protéines de Saccharomyces cerevisiae (métabolisme), Protéines et peptides de signalisation intercellulaire (MeSH), Protéomique (MeSH), Régions promotrices (génétique) (génétique), Saccharomyces cerevisiae (croissance et développement), Saccharomyces cerevisiae (cytologie), Saccharomyces cerevisiae (enzymologie), Sirolimus (pharmacologie), Séquence d'acides aminés (MeSH).
- MESH :
- antagonistes et inhibiteurs : Protein Phosphatase 2.
- composition chimique : Protéines de Saccharomyces cerevisiae.
- croissance et développement : Saccharomyces cerevisiae.
- cytologie : Saccharomyces cerevisiae.
- effets des médicaments et des substances chimiques : Liaison aux protéines, Phosphorylation.
- enzymologie : Saccharomyces cerevisiae.
- génétique : Régions promotrices (génétique).
- métabolisme : Peptides, Protein Phosphatase 2, Protéines de Saccharomyces cerevisiae.
- pharmacologie : Sirolimus.
- Coloration et marquage, Données de séquences moléculaires, Protéines et peptides de signalisation intercellulaire, Protéomique, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Intercellular Signaling Peptides and Proteins (MeSH), Molecular Sequence Data (MeSH), Peptides (metabolism), Phosphorylation (drug effects), Promoter Regions, Genetic (genetics), Protein Binding (drug effects), Protein Phosphatase 2 (antagonists & inhibitors), Protein Phosphatase 2 (metabolism), Proteomics (MeSH), Saccharomyces cerevisiae (cytology), Saccharomyces cerevisiae (enzymology), Saccharomyces cerevisiae (growth & development), Saccharomyces cerevisiae Proteins (chemistry), Saccharomyces cerevisiae Proteins (metabolism), Sirolimus (pharmacology), Staining and Labeling (MeSH).
- MESH :
- chemical , antagonists & inhibitors : Protein Phosphatase 2.
- chemical , chemistry : Saccharomyces cerevisiae Proteins.
- chemical , metabolism : Peptides, Protein Phosphatase 2, Saccharomyces cerevisiae Proteins.
- chemical , pharmacology : Sirolimus.
- chemical : Intercellular Signaling Peptides and Proteins.
- cytology : Saccharomyces cerevisiae.
- drug effects : Phosphorylation, Protein Binding.
- enzymology : Saccharomyces cerevisiae.
- genetics : Promoter Regions, Genetic.
- growth & development : Saccharomyces cerevisiae.
- Amino Acid Sequence, Molecular Sequence Data, Proteomics, Staining and Labeling.
Abstract
The TORC1 and PKA protein kinases are central elements of signaling networks that regulate eukaryotic cell proliferation in response to growth factors and/or nutrients. In yeast, attenuation of signaling by these kinases following nitrogen and/or carbon limitation activates the protein kinase Rim15, which orchestrates the initiation of a reversible cellular quiescence program to ensure normal chronological life span. The molecular elements linking Rim15 to distal readouts including the expression of Msn2/4- and Gis1-dependent genes involve the endosulfines Igo1/2. Here, we show that Rim15, analogous to the greatwall kinase in Xenopus, phosphorylates endosulfines to directly inhibit the Cdc55-protein phosphatase 2A (PP2A(Cdc55)). Inhibition of PP2A(Cdc55) preserves Gis1 in a phosphorylated state and consequently promotes its recruitment to and activation of transcription from promoters of specific nutrient-regulated genes. These results close a gap in our perception of and delineate a role for PP2A(Cdc55) in TORC1-/PKA-mediated regulation of quiescence and chronological life span.
DOI: 10.1016/j.celrep.2012.11.025
PubMed: 23273919
Affiliations:
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In yeast, attenuation of signaling by these kinases following nitrogen and/or carbon limitation activates the protein kinase Rim15, which orchestrates the initiation of a reversible cellular quiescence program to ensure normal chronological life span. The molecular elements linking Rim15 to distal readouts including the expression of Msn2/4- and Gis1-dependent genes involve the endosulfines Igo1/2. Here, we show that Rim15, analogous to the greatwall kinase in Xenopus, phosphorylates endosulfines to directly inhibit the Cdc55-protein phosphatase 2A (PP2A(Cdc55)). Inhibition of PP2A(Cdc55) preserves Gis1 in a phosphorylated state and consequently promotes its recruitment to and activation of transcription from promoters of specific nutrient-regulated genes. These results close a gap in our perception of and delineate a role for PP2A(Cdc55) in TORC1-/PKA-mediated regulation of quiescence and chronological life span.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">23273919</PMID><DateCompleted><Year>2013</Year><Month>07</Month><Day>16</Day></DateCompleted><DateRevised><Year>2019</Year><Month>12</Month><Day>10</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">2211-1247</ISSN><JournalIssue CitedMedium="Internet"><Volume>3</Volume><Issue>1</Issue><PubDate><Year>2013</Year><Month>Jan</Month><Day>31</Day></PubDate></JournalIssue><Title>Cell reports</Title><ISOAbbreviation>Cell Rep</ISOAbbreviation></Journal><ArticleTitle>Yeast endosulfines control entry into quiescence and chronological life span by inhibiting protein phosphatase 2A.</ArticleTitle><Pagination><MedlinePgn>16-22</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.celrep.2012.11.025</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S2211-1247(12)00422-6</ELocationID><Abstract><AbstractText>The TORC1 and PKA protein kinases are central elements of signaling networks that regulate eukaryotic cell proliferation in response to growth factors and/or nutrients. In yeast, attenuation of signaling by these kinases following nitrogen and/or carbon limitation activates the protein kinase Rim15, which orchestrates the initiation of a reversible cellular quiescence program to ensure normal chronological life span. The molecular elements linking Rim15 to distal readouts including the expression of Msn2/4- and Gis1-dependent genes involve the endosulfines Igo1/2. Here, we show that Rim15, analogous to the greatwall kinase in Xenopus, phosphorylates endosulfines to directly inhibit the Cdc55-protein phosphatase 2A (PP2A(Cdc55)). Inhibition of PP2A(Cdc55) preserves Gis1 in a phosphorylated state and consequently promotes its recruitment to and activation of transcription from promoters of specific nutrient-regulated genes. These results close a gap in our perception of and delineate a role for PP2A(Cdc55) in TORC1-/PKA-mediated regulation of quiescence and chronological life span.</AbstractText><CopyrightInformation>Copyright © 2013 The Authors. 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UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000166" MajorTopicYN="N">cytology</QualifierName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000254" MajorTopicYN="Y">growth & development</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029701" MajorTopicYN="N">Saccharomyces cerevisiae Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020123" MajorTopicYN="N">Sirolimus</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013194" MajorTopicYN="N">Staining and Labeling</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2012</Year><Month>09</Month><Day>12</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2012</Year><Month>11</Month><Day>12</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2012</Year><Month>11</Month><Day>28</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2013</Year><Month>1</Month><Day>1</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2013</Year><Month>1</Month><Day>1</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2013</Year><Month>7</Month><Day>17</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">23273919</ArticleId><ArticleId IdType="pii">S2211-1247(12)00422-6</ArticleId><ArticleId IdType="doi">10.1016/j.celrep.2012.11.025</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Suisse</li></country><region><li>Canton de Fribourg</li></region><settlement><li>Fribourg</li></settlement><orgName><li>Université de Fribourg</li></orgName></list><tree><noCountry><name sortKey="Aebersold, Ruedi" sort="Aebersold, Ruedi" uniqKey="Aebersold R" first="Ruedi" last="Aebersold">Ruedi Aebersold</name><name sortKey="Bodenmiller, Bernd" sort="Bodenmiller, Bernd" uniqKey="Bodenmiller B" first="Bernd" last="Bodenmiller">Bernd Bodenmiller</name><name sortKey="De Virgilio, Claudio" sort="De Virgilio, Claudio" uniqKey="De Virgilio C" first="Claudio" last="De Virgilio">Claudio De Virgilio</name><name sortKey="Jaquenoud, Malika" sort="Jaquenoud, Malika" uniqKey="Jaquenoud M" first="Malika" last="Jaquenoud">Malika Jaquenoud</name><name sortKey="Talarek, Nicolas" sort="Talarek, Nicolas" uniqKey="Talarek N" first="Nicolas" last="Talarek">Nicolas Talarek</name><name sortKey="Vaga, Stefania" sort="Vaga, Stefania" uniqKey="Vaga S" first="Stefania" last="Vaga">Stefania Vaga</name></noCountry><country name="Suisse"><region name="Canton de Fribourg"><name sortKey="Bontron, Severine" sort="Bontron, Severine" uniqKey="Bontron S" first="Séverine" last="Bontron">Séverine Bontron</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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