TORC1 and TORC2 converge to regulate the SAGA co-activator in response to nutrient availability.
Identifieur interne : 000347 ( PubMed/Corpus ); précédent : 000346; suivant : 000348TORC1 and TORC2 converge to regulate the SAGA co-activator in response to nutrient availability.
Auteurs : Thomas Laboucarié ; Dylane Detilleux ; Ricard A. Rodriguez-Mias ; Céline Faux ; Yves Romeo ; Mirita Franz-Wachtel ; Karsten Krug ; Boris Ma Ek ; Judit Villén ; Janni Petersen ; Dominique HelmlingerSource :
- EMBO reports [ 1469-3178 ] ; 2017.
Abstract
Gene expression regulation is essential for cells to adapt to changes in their environment. Co-activator complexes have well-established roles in transcriptional regulation, but less is known about how they sense and respond to signaling cues. We have previously shown that, in fission yeast, one such co-activator, the SAGA complex, controls gene expression and the switch from proliferation to differentiation in response to nutrient availability. Here, using a combination of genetic, biochemical, and proteomic approaches, we show that SAGA responds to nutrients through the differential phosphorylation of its Taf12 component, downstream of both the TORC1 and TORC2 pathways. Taf12 phosphorylation increases early upon starvation and is controlled by the opposing activities of the PP2A phosphatase, which is activated by TORC1, and the TORC2-activated Gad8(AKT) kinase. Mutational analyses suggest that Taf12 phosphorylation prevents cells from committing to differentiation until starvation reaches a critical level. Overall, our work reveals that SAGA is a direct target of nutrient-sensing pathways and has uncovered a mechanism by which TORC1 and TORC2 converge to control gene expression and cell fate decisions.
DOI: 10.15252/embr.201744942
PubMed: 29079657
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Rodriguez-Mias</name><affiliation><nlm:affiliation>Department of Genome Sciences, University of Washington, Seattle, WA, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Faux, Celine" sort="Faux, Celine" uniqKey="Faux C" first="Céline" last="Faux">Céline Faux</name><affiliation><nlm:affiliation>CRBM, CNRS, University of Montpellier, Montpellier, France.</nlm:affiliation></affiliation></author><author><name sortKey="Romeo, Yves" sort="Romeo, Yves" uniqKey="Romeo Y" first="Yves" last="Romeo">Yves Romeo</name><affiliation><nlm:affiliation>CRBM, CNRS, University of Montpellier, Montpellier, France.</nlm:affiliation></affiliation></author><author><name sortKey="Franz Wachtel, Mirita" sort="Franz Wachtel, Mirita" uniqKey="Franz Wachtel M" first="Mirita" last="Franz-Wachtel">Mirita Franz-Wachtel</name><affiliation><nlm:affiliation>Proteome Center Tübingen, Tuebingen, Germany.</nlm:affiliation></affiliation></author><author><name sortKey="Krug, Karsten" sort="Krug, Karsten" uniqKey="Krug K" first="Karsten" last="Krug">Karsten Krug</name><affiliation><nlm:affiliation>Proteome Center Tübingen, Tuebingen, Germany.</nlm:affiliation></affiliation></author><author><name sortKey="Ma Ek, Boris" sort="Ma Ek, Boris" uniqKey="Ma Ek B" first="Boris" last="Ma Ek">Boris Ma Ek</name><affiliation><nlm:affiliation>Proteome Center Tübingen, Tuebingen, Germany.</nlm:affiliation></affiliation></author><author><name sortKey="Villen, Judit" sort="Villen, Judit" uniqKey="Villen J" first="Judit" last="Villén">Judit Villén</name><affiliation><nlm:affiliation>Department of Genome Sciences, University of Washington, Seattle, WA, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Petersen, Janni" sort="Petersen, Janni" uniqKey="Petersen J" first="Janni" last="Petersen">Janni Petersen</name><affiliation><nlm:affiliation>Flinders Centre for Innovation in Cancer, School of Medicine, Faculty of Health Science, Flinders University, Adelaide, SA, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Helmlinger, Dominique" sort="Helmlinger, Dominique" uniqKey="Helmlinger D" first="Dominique" last="Helmlinger">Dominique Helmlinger</name><affiliation><nlm:affiliation>CRBM, CNRS, University of Montpellier, Montpellier, France dhelmlinger@crbm.cnrs.fr.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2017">2017</date><idno type="RBID">pubmed:29079657</idno><idno type="pmid">29079657</idno><idno type="doi">10.15252/embr.201744942</idno><idno type="wicri:Area/PubMed/Corpus">000347</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000347</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">TORC1 and TORC2 converge to regulate the SAGA co-activator in response to nutrient availability.</title><author><name sortKey="Laboucarie, Thomas" sort="Laboucarie, Thomas" uniqKey="Laboucarie T" first="Thomas" last="Laboucarié">Thomas Laboucarié</name><affiliation><nlm:affiliation>CRBM, CNRS, University of Montpellier, Montpellier, France.</nlm:affiliation></affiliation></author><author><name sortKey="Detilleux, Dylane" sort="Detilleux, Dylane" uniqKey="Detilleux D" first="Dylane" last="Detilleux">Dylane Detilleux</name><affiliation><nlm:affiliation>CRBM, CNRS, University of Montpellier, Montpellier, France.</nlm:affiliation></affiliation></author><author><name sortKey="Rodriguez Mias, Ricard A" sort="Rodriguez Mias, Ricard A" uniqKey="Rodriguez Mias R" first="Ricard A" last="Rodriguez-Mias">Ricard A. Rodriguez-Mias</name><affiliation><nlm:affiliation>Department of Genome Sciences, University of Washington, Seattle, WA, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Faux, Celine" sort="Faux, Celine" uniqKey="Faux C" first="Céline" last="Faux">Céline Faux</name><affiliation><nlm:affiliation>CRBM, CNRS, University of Montpellier, Montpellier, France.</nlm:affiliation></affiliation></author><author><name sortKey="Romeo, Yves" sort="Romeo, Yves" uniqKey="Romeo Y" first="Yves" last="Romeo">Yves Romeo</name><affiliation><nlm:affiliation>CRBM, CNRS, University of Montpellier, Montpellier, France.</nlm:affiliation></affiliation></author><author><name sortKey="Franz Wachtel, Mirita" sort="Franz Wachtel, Mirita" uniqKey="Franz Wachtel M" first="Mirita" last="Franz-Wachtel">Mirita Franz-Wachtel</name><affiliation><nlm:affiliation>Proteome Center Tübingen, Tuebingen, Germany.</nlm:affiliation></affiliation></author><author><name sortKey="Krug, Karsten" sort="Krug, Karsten" uniqKey="Krug K" first="Karsten" last="Krug">Karsten Krug</name><affiliation><nlm:affiliation>Proteome Center Tübingen, Tuebingen, Germany.</nlm:affiliation></affiliation></author><author><name sortKey="Ma Ek, Boris" sort="Ma Ek, Boris" uniqKey="Ma Ek B" first="Boris" last="Ma Ek">Boris Ma Ek</name><affiliation><nlm:affiliation>Proteome Center Tübingen, Tuebingen, Germany.</nlm:affiliation></affiliation></author><author><name sortKey="Villen, Judit" sort="Villen, Judit" uniqKey="Villen J" first="Judit" last="Villén">Judit Villén</name><affiliation><nlm:affiliation>Department of Genome Sciences, University of Washington, Seattle, WA, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Petersen, Janni" sort="Petersen, Janni" uniqKey="Petersen J" first="Janni" last="Petersen">Janni Petersen</name><affiliation><nlm:affiliation>Flinders Centre for Innovation in Cancer, School of Medicine, Faculty of Health Science, Flinders University, Adelaide, SA, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Helmlinger, Dominique" sort="Helmlinger, Dominique" uniqKey="Helmlinger D" first="Dominique" last="Helmlinger">Dominique Helmlinger</name><affiliation><nlm:affiliation>CRBM, CNRS, University of Montpellier, Montpellier, France dhelmlinger@crbm.cnrs.fr.</nlm:affiliation></affiliation></author></analytic><series><title level="j">EMBO reports</title><idno type="eISSN">1469-3178</idno><imprint><date when="2017" type="published">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Gene expression regulation is essential for cells to adapt to changes in their environment. Co-activator complexes have well-established roles in transcriptional regulation, but less is known about how they sense and respond to signaling cues. We have previously shown that, in fission yeast, one such co-activator, the SAGA complex, controls gene expression and the switch from proliferation to differentiation in response to nutrient availability. Here, using a combination of genetic, biochemical, and proteomic approaches, we show that SAGA responds to nutrients through the differential phosphorylation of its Taf12 component, downstream of both the TORC1 and TORC2 pathways. Taf12 phosphorylation increases early upon starvation and is controlled by the opposing activities of the PP2A phosphatase, which is activated by TORC1, and the TORC2-activated Gad8(AKT) kinase. Mutational analyses suggest that Taf12 phosphorylation prevents cells from committing to differentiation until starvation reaches a critical level. Overall, our work reveals that SAGA is a direct target of nutrient-sensing pathways and has uncovered a mechanism by which TORC1 and TORC2 converge to control gene expression and cell fate decisions.</div></front></TEI><pubmed><MedlineCitation Status="Publisher" Owner="NLM"><PMID Version="1">29079657</PMID><DateCreated><Year>2017</Year><Month>10</Month><Day>28</Day></DateCreated><DateRevised><Year>2017</Year><Month>10</Month><Day>28</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1469-3178</ISSN><JournalIssue CitedMedium="Internet"><PubDate><Year>2017</Year><Month>Oct</Month><Day>27</Day></PubDate></JournalIssue><Title>EMBO reports</Title><ISOAbbreviation>EMBO Rep.</ISOAbbreviation></Journal><ArticleTitle>TORC1 and TORC2 converge to regulate the SAGA co-activator in response to nutrient availability.</ArticleTitle><ELocationID EIdType="pii" ValidYN="Y">e201744942</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.15252/embr.201744942</ELocationID><Abstract><AbstractText>Gene expression regulation is essential for cells to adapt to changes in their environment. Co-activator complexes have well-established roles in transcriptional regulation, but less is known about how they sense and respond to signaling cues. We have previously shown that, in fission yeast, one such co-activator, the SAGA complex, controls gene expression and the switch from proliferation to differentiation in response to nutrient availability. Here, using a combination of genetic, biochemical, and proteomic approaches, we show that SAGA responds to nutrients through the differential phosphorylation of its Taf12 component, downstream of both the TORC1 and TORC2 pathways. Taf12 phosphorylation increases early upon starvation and is controlled by the opposing activities of the PP2A phosphatase, which is activated by TORC1, and the TORC2-activated Gad8(AKT) kinase. Mutational analyses suggest that Taf12 phosphorylation prevents cells from committing to differentiation until starvation reaches a critical level. Overall, our work reveals that SAGA is a direct target of nutrient-sensing pathways and has uncovered a mechanism by which TORC1 and TORC2 converge to control gene expression and cell fate decisions.</AbstractText><CopyrightInformation>© 2017 The Authors.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Laboucarié</LastName><ForeName>Thomas</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>CRBM, CNRS, University of Montpellier, Montpellier, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Detilleux</LastName><ForeName>Dylane</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>CRBM, CNRS, University of Montpellier, Montpellier, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Rodriguez-Mias</LastName><ForeName>Ricard A</ForeName><Initials>RA</Initials><AffiliationInfo><Affiliation>Department of Genome Sciences, University of Washington, Seattle, WA, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Faux</LastName><ForeName>Céline</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>CRBM, CNRS, University of Montpellier, Montpellier, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Romeo</LastName><ForeName>Yves</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>CRBM, CNRS, University of Montpellier, Montpellier, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Franz-Wachtel</LastName><ForeName>Mirita</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Proteome Center Tübingen, Tuebingen, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Krug</LastName><ForeName>Karsten</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Proteome Center Tübingen, Tuebingen, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Maček</LastName><ForeName>Boris</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Proteome Center Tübingen, Tuebingen, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Villén</LastName><ForeName>Judit</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Department of Genome Sciences, University of Washington, Seattle, WA, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Petersen</LastName><ForeName>Janni</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Flinders Centre for Innovation in Cancer, School of Medicine, Faculty of Health Science, Flinders University, Adelaide, SA, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Helmlinger</LastName><ForeName>Dominique</ForeName><Initials>D</Initials><Identifier Source="ORCID">http://orcid.org/0000-0003-1501-0423</Identifier><AffiliationInfo><Affiliation>CRBM, CNRS, University of Montpellier, Montpellier, France dhelmlinger@crbm.cnrs.fr.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2017</Year><Month>10</Month><Day>27</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>EMBO Rep</MedlineTA><NlmUniqueID>100963049</NlmUniqueID><ISSNLinking>1469-221X</ISSNLinking></MedlineJournalInfo><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">SAGA</Keyword><Keyword MajorTopicYN="N">TOR</Keyword><Keyword MajorTopicYN="N">differentiation</Keyword><Keyword MajorTopicYN="N">fission yeast</Keyword><Keyword MajorTopicYN="N">signal transduction</Keyword><Keyword MajorTopicYN="N">transcription</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2017</Year><Month>07</Month><Day>31</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2017</Year><Month>08</Month><Day>31</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2017</Year><Month>09</Month><Day>07</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2017</Year><Month>10</Month><Day>29</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2017</Year><Month>10</Month><Day>29</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2017</Year><Month>10</Month><Day>29</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>aheadofprint</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">29079657</ArticleId><ArticleId IdType="pii">embr.201744942</ArticleId><ArticleId IdType="doi">10.15252/embr.201744942</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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