Sphingolipid/Pkh1/2-TORC1/Sch9 Signaling Regulates Ribosome Biogenesis in Tunicamycin-Induced Stress Response in Yeast.
Identifieur interne : 000229 ( Main/Exploration ); précédent : 000228; suivant : 000230Sphingolipid/Pkh1/2-TORC1/Sch9 Signaling Regulates Ribosome Biogenesis in Tunicamycin-Induced Stress Response in Yeast.
Auteurs : Yukari Yabuki [Japon] ; Atsuko Ikeda [Japon] ; Misako Araki [Japon] ; Kentaro Kajiwara [Japon] ; Keiko Mizuta [Japon] ; Kouichi Funato [Japon]Source :
- Genetics [ 1943-2631 ] ; 2019.
Descripteurs français
- KwdFr :
- 3-Phosphoinositide-dependent protein kinases (métabolisme), Facteurs de transcription (métabolisme), Protein-Serine-Threonine Kinases (métabolisme), Protéines de Saccharomyces cerevisiae (métabolisme), Ribosomes (métabolisme), Régulation de l'expression des gènes fongiques (MeSH), Saccharomyces cerevisiae (effets des médicaments et des substances chimiques), Saccharomyces cerevisiae (génétique), Saccharomyces cerevisiae (métabolisme), Sphingolipides (métabolisme), Stress du réticulum endoplasmique (effets des médicaments et des substances chimiques), Transduction du signal (MeSH), Tunicamycine (pharmacologie), Tunicamycine (toxicité).
- MESH :
- effets des médicaments et des substances chimiques : Saccharomyces cerevisiae, Stress du réticulum endoplasmique.
- génétique : Saccharomyces cerevisiae.
- métabolisme : 3-Phosphoinositide-dependent protein kinases, Facteurs de transcription, Protein-Serine-Threonine Kinases, Protéines de Saccharomyces cerevisiae, Ribosomes, Saccharomyces cerevisiae, Sphingolipides.
- pharmacologie : Tunicamycine.
- toxicité : Tunicamycine.
- Régulation de l'expression des gènes fongiques, Transduction du signal.
English descriptors
- KwdEn :
- 3-Phosphoinositide-Dependent Protein Kinases (metabolism), Endoplasmic Reticulum Stress (drug effects), Gene Expression Regulation, Fungal (MeSH), Protein-Serine-Threonine Kinases (metabolism), Ribosomes (metabolism), Saccharomyces cerevisiae (drug effects), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (metabolism), Signal Transduction (MeSH), Sphingolipids (metabolism), Transcription Factors (metabolism), Tunicamycin (pharmacology), Tunicamycin (toxicity).
- MESH :
- chemical , metabolism : 3-Phosphoinositide-Dependent Protein Kinases, Protein-Serine-Threonine Kinases, Saccharomyces cerevisiae Proteins, Sphingolipids, Transcription Factors.
- drug effects : Endoplasmic Reticulum Stress, Saccharomyces cerevisiae.
- genetics : Saccharomyces cerevisiae.
- metabolism : Ribosomes, Saccharomyces cerevisiae.
- chemical , pharmacology : Tunicamycin.
- chemical , toxicity : Tunicamycin.
- Gene Expression Regulation, Fungal, Signal Transduction.
Abstract
Reduced ribosome biogenesis in response to environmental conditions is a key feature of cell adaptation to stress. For example, ribosomal genes are transcriptionally repressed when cells are exposed to tunicamycin, a protein glycosylation inhibitor that induces endoplasmic reticulum stress and blocks vesicular trafficking in the secretory pathway. Here, we describe a novel regulatory model, in which tunicamycin-mediated stress induces the accumulation of long-chain sphingoid bases and subsequent activation of Pkh1/2 signaling, which leads to decreased expression of ribosomal protein genes via the downstream effectors Pkc1 and Sch9. Target of rapamycin complex 1 (TORC1), an upstream activator of Sch9, is also required. This pathway links ribosome biogenesis to alterations in membrane lipid composition under tunicamycin-induced stress conditions. Our results suggest that sphingolipid/Pkh1/2-TORC1/Sch9 signaling is an important determinant for adaptation to tunicamycin-induced stress.
DOI: 10.1534/genetics.118.301874
PubMed: 30824472
PubMed Central: PMC6499531
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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last="Yabuki">Yukari Yabuki</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biofunctional Science and Technology, Graduate School of Biosphere Science, Hiroshima University, Higashi-Hiroshima 739-8528, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Biofunctional Science and Technology, Graduate School of Biosphere Science, Hiroshima University, Higashi-Hiroshima 739-8528</wicri:regionArea><wicri:noRegion>Higashi-Hiroshima 739-8528</wicri:noRegion></affiliation></author><author><name sortKey="Ikeda, Atsuko" sort="Ikeda, Atsuko" uniqKey="Ikeda A" first="Atsuko" last="Ikeda">Atsuko Ikeda</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biofunctional Science and Technology, Graduate School of Biosphere Science, Hiroshima University, Higashi-Hiroshima 739-8528, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Biofunctional Science and Technology, Graduate School of 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739-8528</wicri:regionArea><wicri:noRegion>Higashi-Hiroshima 739-8528</wicri:noRegion></affiliation></author><author><name sortKey="Funato, Kouichi" sort="Funato, Kouichi" uniqKey="Funato K" first="Kouichi" last="Funato">Kouichi Funato</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biofunctional Science and Technology, Graduate School of Biosphere Science, Hiroshima University, Higashi-Hiroshima 739-8528, Japan kfunato@hiroshima-u.ac.jp.</nlm:affiliation><country wicri:rule="url">Japon</country><wicri:regionArea>Department of Biofunctional Science and Technology, Graduate School of Biosphere Science, Hiroshima University, Higashi-Hiroshima 739-8528</wicri:regionArea><wicri:noRegion>Higashi-Hiroshima 739-8528</wicri:noRegion></affiliation></author></analytic><series><title level="j">Genetics</title><idno type="eISSN">1943-2631</idno><imprint><date when="2019" type="published">2019</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>3-Phosphoinositide-Dependent Protein Kinases (metabolism)</term><term>Endoplasmic Reticulum Stress (drug effects)</term><term>Gene Expression Regulation, Fungal (MeSH)</term><term>Protein-Serine-Threonine Kinases (metabolism)</term><term>Ribosomes (metabolism)</term><term>Saccharomyces cerevisiae (drug effects)</term><term>Saccharomyces cerevisiae (genetics)</term><term>Saccharomyces cerevisiae (metabolism)</term><term>Saccharomyces cerevisiae Proteins (metabolism)</term><term>Signal Transduction (MeSH)</term><term>Sphingolipids (metabolism)</term><term>Transcription Factors (metabolism)</term><term>Tunicamycin (pharmacology)</term><term>Tunicamycin (toxicity)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>3-Phosphoinositide-dependent protein kinases (métabolisme)</term><term>Facteurs de transcription (métabolisme)</term><term>Protein-Serine-Threonine Kinases (métabolisme)</term><term>Protéines de Saccharomyces cerevisiae (métabolisme)</term><term>Ribosomes (métabolisme)</term><term>Régulation de l'expression des gènes fongiques (MeSH)</term><term>Saccharomyces cerevisiae (effets des médicaments et des substances chimiques)</term><term>Saccharomyces cerevisiae (génétique)</term><term>Saccharomyces cerevisiae (métabolisme)</term><term>Sphingolipides (métabolisme)</term><term>Stress du réticulum endoplasmique (effets des médicaments et des substances chimiques)</term><term>Transduction du signal (MeSH)</term><term>Tunicamycine (pharmacologie)</term><term>Tunicamycine (toxicité)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>3-Phosphoinositide-Dependent Protein Kinases</term><term>Protein-Serine-Threonine Kinases</term><term>Saccharomyces cerevisiae Proteins</term><term>Sphingolipids</term><term>Transcription Factors</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Endoplasmic Reticulum Stress</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Saccharomyces cerevisiae</term><term>Stress du réticulum endoplasmique</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Ribosomes</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>3-Phosphoinositide-dependent protein kinases</term><term>Facteurs de transcription</term><term>Protein-Serine-Threonine Kinases</term><term>Protéines de Saccharomyces cerevisiae</term><term>Ribosomes</term><term>Saccharomyces cerevisiae</term><term>Sphingolipides</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Tunicamycine</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Tunicamycin</term></keywords><keywords scheme="MESH" type="chemical" qualifier="toxicity" xml:lang="en"><term>Tunicamycin</term></keywords><keywords scheme="MESH" qualifier="toxicité" xml:lang="fr"><term>Tunicamycine</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Gene Expression Regulation, Fungal</term><term>Signal Transduction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Régulation de l'expression des gènes fongiques</term><term>Transduction du signal</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Reduced ribosome biogenesis in response to environmental conditions is a key feature of cell adaptation to stress. For example, ribosomal genes are transcriptionally repressed when cells are exposed to tunicamycin, a protein glycosylation inhibitor that induces endoplasmic reticulum stress and blocks vesicular trafficking in the secretory pathway. Here, we describe a novel regulatory model, in which tunicamycin-mediated stress induces the accumulation of long-chain sphingoid bases and subsequent activation of Pkh1/2 signaling, which leads to decreased expression of ribosomal protein genes via the downstream effectors Pkc1 and Sch9. Target of rapamycin complex 1 (TORC1), an upstream activator of Sch9, is also required. This pathway links ribosome biogenesis to alterations in membrane lipid composition under tunicamycin-induced stress conditions. Our results suggest that sphingolipid/Pkh1/2-TORC1/Sch9 signaling is an important determinant for adaptation to tunicamycin-induced stress.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">30824472</PMID><DateCompleted><Year>2019</Year><Month>09</Month><Day>03</Day></DateCompleted><DateRevised><Year>2020</Year><Month>05</Month><Day>01</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1943-2631</ISSN><JournalIssue CitedMedium="Internet"><Volume>212</Volume><Issue>1</Issue><PubDate><Year>2019</Year><Month>05</Month></PubDate></JournalIssue><Title>Genetics</Title><ISOAbbreviation>Genetics</ISOAbbreviation></Journal><ArticleTitle>Sphingolipid/Pkh1/2-TORC1/Sch9 Signaling Regulates Ribosome Biogenesis in Tunicamycin-Induced Stress Response in Yeast.</ArticleTitle><Pagination><MedlinePgn>175-186</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1534/genetics.118.301874</ELocationID><Abstract><AbstractText>Reduced ribosome biogenesis in response to environmental conditions is a key feature of cell adaptation to stress. For example, ribosomal genes are transcriptionally repressed when cells are exposed to tunicamycin, a protein glycosylation inhibitor that induces endoplasmic reticulum stress and blocks vesicular trafficking in the secretory pathway. Here, we describe a novel regulatory model, in which tunicamycin-mediated stress induces the accumulation of long-chain sphingoid bases and subsequent activation of Pkh1/2 signaling, which leads to decreased expression of ribosomal protein genes via the downstream effectors Pkc1 and Sch9. Target of rapamycin complex 1 (TORC1), an upstream activator of Sch9, is also required. This pathway links ribosome biogenesis to alterations in membrane lipid composition under tunicamycin-induced stress conditions. Our results suggest that sphingolipid/Pkh1/2-TORC1/Sch9 signaling is an important determinant for adaptation to tunicamycin-induced stress.</AbstractText><CopyrightInformation>Copyright © 2019 by the Genetics Society of America.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Yabuki</LastName><ForeName>Yukari</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Department of Biofunctional Science and Technology, Graduate School of Biosphere Science, Hiroshima University, Higashi-Hiroshima 739-8528, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ikeda</LastName><ForeName>Atsuko</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Department of Biofunctional Science and Technology, Graduate School of Biosphere Science, Hiroshima University, Higashi-Hiroshima 739-8528, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Araki</LastName><ForeName>Misako</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Department of Biofunctional Science and Technology, Graduate School of Biosphere Science, Hiroshima University, Higashi-Hiroshima 739-8528, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kajiwara</LastName><ForeName>Kentaro</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Department of Biofunctional Science and Technology, Graduate School of Biosphere Science, Hiroshima University, Higashi-Hiroshima 739-8528, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mizuta</LastName><ForeName>Keiko</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Department of Biofunctional Science and Technology, Graduate School of Biosphere Science, Hiroshima University, Higashi-Hiroshima 739-8528, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Funato</LastName><ForeName>Kouichi</ForeName><Initials>K</Initials><Identifier Source="ORCID">0000-0002-1486-1296</Identifier><AffiliationInfo><Affiliation>Department of Biofunctional Science and Technology, Graduate School of Biosphere Science, Hiroshima University, Higashi-Hiroshima 739-8528, Japan kfunato@hiroshima-u.ac.jp.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2019</Year><Month>03</Month><Day>01</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Genetics</MedlineTA><NlmUniqueID>0374636</NlmUniqueID><ISSNLinking>0016-6731</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029701">Saccharomyces cerevisiae Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D013107">Sphingolipids</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C561842">TORC1 protein complex, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014157">Transcription Factors</NameOfSubstance></Chemical><Chemical><RegistryNumber>11089-65-9</RegistryNumber><NameOfSubstance UI="D014415">Tunicamycin</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber><NameOfSubstance UI="D064413">3-Phosphoinositide-Dependent Protein Kinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber><NameOfSubstance UI="C118385">PKH1 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber><NameOfSubstance UI="C118386">PKH2 protein, S cerevisiae</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="C530964">SCH9 protein, S cerevisiae</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D064413" MajorTopicYN="N">3-Phosphoinositide-Dependent Protein Kinases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D059865" MajorTopicYN="N">Endoplasmic Reticulum Stress</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015966" MajorTopicYN="N">Gene Expression Regulation, Fungal</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017346" MajorTopicYN="N">Protein-Serine-Threonine Kinases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012270" MajorTopicYN="N">Ribosomes</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><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="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015398" MajorTopicYN="Y">Signal Transduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013107" MajorTopicYN="N">Sphingolipids</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014157" MajorTopicYN="N">Transcription Factors</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014415" MajorTopicYN="N">Tunicamycin</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName><QualifierName UI="Q000633" MajorTopicYN="N">toxicity</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">TORC1-Sch9</Keyword><Keyword MajorTopicYN="Y">ribosome</Keyword><Keyword MajorTopicYN="Y">sphingolipid-Pkh1/2</Keyword><Keyword MajorTopicYN="Y">stress response</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2018</Year><Month>12</Month><Day>11</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2019</Year><Month>02</Month><Day>26</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2019</Year><Month>3</Month><Day>3</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2019</Year><Month>9</Month><Day>4</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2019</Year><Month>3</Month><Day>3</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">30824472</ArticleId><ArticleId IdType="pii">genetics.118.301874</ArticleId><ArticleId IdType="doi">10.1534/genetics.118.301874</ArticleId><ArticleId IdType="pmc">PMC6499531</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>Curr Biol. 1999 Feb 25;9(4):186-97</Citation><ArticleIdList><ArticleId IdType="pubmed">10074427</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1999 May 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