TORC1 regulates autophagy induction in response to proteotoxic stress in yeast and human cells.
Identifieur interne : 000218 ( Main/Exploration ); précédent : 000217; suivant : 000219TORC1 regulates autophagy induction in response to proteotoxic stress in yeast and human cells.
Auteurs : Kazuki Suda [Japon] ; Atsuki Kaneko [Japon] ; Mitsugu Shimobayashi [Suisse] ; Akio Nakashima [Japon] ; Tatsuya Maeda [Japon] ; Michael N. Hall [Suisse] ; Takashi Ushimaru [Japon]Source :
- Biochemical and biophysical research communications [ 1090-2104 ] ; 2019.
Descripteurs français
- KwdFr :
- Acide azétidine-2-carboxylique (toxicité), Autophagie (effets des médicaments et des substances chimiques), Cellules HEK293 (MeSH), Complexe-1 cible mécanistique de la rapamycine (métabolisme), Humains (MeSH), Protéines fongiques (métabolisme), Saccharomyces cerevisiae (cytologie), Saccharomyces cerevisiae (effets des médicaments et des substances chimiques), Schizosaccharomyces (cytologie), Schizosaccharomyces (effets des médicaments et des substances chimiques).
- MESH :
- cytologie : Saccharomyces cerevisiae, Schizosaccharomyces.
- effets des médicaments et des substances chimiques : Autophagie, Saccharomyces cerevisiae, Schizosaccharomyces.
- métabolisme : Complexe-1 cible mécanistique de la rapamycine, Protéines fongiques.
- toxicité : Acide azétidine-2-carboxylique.
- Cellules HEK293, Humains.
English descriptors
- KwdEn :
- Autophagy (drug effects), Azetidinecarboxylic Acid (toxicity), Fungal Proteins (metabolism), HEK293 Cells (MeSH), Humans (MeSH), Mechanistic Target of Rapamycin Complex 1 (metabolism), Saccharomyces cerevisiae (cytology), Saccharomyces cerevisiae (drug effects), Schizosaccharomyces (cytology), Schizosaccharomyces (drug effects).
- MESH :
- chemical , metabolism : Fungal Proteins, Mechanistic Target of Rapamycin Complex 1.
- chemical , toxicity : Azetidinecarboxylic Acid.
- cytology : Saccharomyces cerevisiae, Schizosaccharomyces.
- drug effects : Autophagy, Saccharomyces cerevisiae, Schizosaccharomyces.
- HEK293 Cells, Humans.
Abstract
Misfolded and aggregated proteins are eliminated to maintain protein homeostasis. Autophagy contributes to the removal of protein aggregates. However, if and how proteotoxic stress induces autophagy is poorly understood. Here we show that proteotoxic stress after treatment with azetidine-2-carboxylic acid (AZC), a toxic proline analog, induces autophagy in budding yeast. AZC treatment attenuated target of rapamycin complex 1 (TORC1) activity, resulting in the dephosphorylation of Atg13, a key factor of autophagy. By contrast, AZC treatment did not affect target of rapamycin complex 2 (TORC2). Proteotoxic stress also induced TORC1 inactivation and autophagy in fission yeast and human cells. This study suggested that TORC1 is a conserved key factor to cope with proteotoxic stress in eukaryotic cells.
DOI: 10.1016/j.bbrc.2019.02.077
PubMed: 30797551
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Hall</name><affiliation wicri:level="1"><nlm:affiliation>Biozentrum, University of Basel, 4056, Basel, Switzerland, Switzerland.</nlm:affiliation><country xml:lang="fr">Suisse</country><wicri:regionArea>Biozentrum, University of Basel, 4056, Basel, Switzerland</wicri:regionArea><wicri:noRegion>Switzerland</wicri:noRegion></affiliation></author><author><name sortKey="Ushimaru, Takashi" sort="Ushimaru, Takashi" uniqKey="Ushimaru T" first="Takashi" last="Ushimaru">Takashi Ushimaru</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biological Science, Shizuoka University, Shizuoka, 422-8021, Japan; Course of Biological Science, Department of Science, Graduate School of Integrated Science and Technology, Shizuoka University, Shizuoka, 422-8021, Japan. Electronic address: ushimaru.takashi@shizuoka.ac.jp.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Biological Science, Shizuoka University, Shizuoka, 422-8021, Japan; Course of Biological Science, Department of Science, Graduate School of Integrated Science and Technology, Shizuoka University, Shizuoka, 422-8021</wicri:regionArea><wicri:noRegion>422-8021</wicri:noRegion></affiliation></author></analytic><series><title level="j">Biochemical and biophysical research communications</title><idno type="eISSN">1090-2104</idno><imprint><date when="2019" type="published">2019</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Autophagy (drug effects)</term><term>Azetidinecarboxylic Acid (toxicity)</term><term>Fungal Proteins (metabolism)</term><term>HEK293 Cells (MeSH)</term><term>Humans (MeSH)</term><term>Mechanistic Target of Rapamycin Complex 1 (metabolism)</term><term>Saccharomyces cerevisiae (cytology)</term><term>Saccharomyces cerevisiae (drug effects)</term><term>Schizosaccharomyces (cytology)</term><term>Schizosaccharomyces (drug effects)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acide azétidine-2-carboxylique (toxicité)</term><term>Autophagie (effets des médicaments et des substances chimiques)</term><term>Cellules HEK293 (MeSH)</term><term>Complexe-1 cible mécanistique de la rapamycine (métabolisme)</term><term>Humains (MeSH)</term><term>Protéines fongiques (métabolisme)</term><term>Saccharomyces cerevisiae (cytologie)</term><term>Saccharomyces cerevisiae (effets des médicaments et des substances chimiques)</term><term>Schizosaccharomyces (cytologie)</term><term>Schizosaccharomyces (effets des médicaments et des substances chimiques)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Fungal Proteins</term><term>Mechanistic Target of Rapamycin Complex 1</term></keywords><keywords scheme="MESH" type="chemical" qualifier="toxicity" xml:lang="en"><term>Azetidinecarboxylic Acid</term></keywords><keywords scheme="MESH" qualifier="cytologie" xml:lang="fr"><term>Saccharomyces cerevisiae</term><term>Schizosaccharomyces</term></keywords><keywords scheme="MESH" qualifier="cytology" xml:lang="en"><term>Saccharomyces cerevisiae</term><term>Schizosaccharomyces</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Autophagy</term><term>Saccharomyces cerevisiae</term><term>Schizosaccharomyces</term></keywords><keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Autophagie</term><term>Saccharomyces cerevisiae</term><term>Schizosaccharomyces</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Complexe-1 cible mécanistique de la rapamycine</term><term>Protéines fongiques</term></keywords><keywords scheme="MESH" qualifier="toxicité" xml:lang="fr"><term>Acide azétidine-2-carboxylique</term></keywords><keywords scheme="MESH" xml:lang="en"><term>HEK293 Cells</term><term>Humans</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cellules HEK293</term><term>Humains</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Misfolded and aggregated proteins are eliminated to maintain protein homeostasis. Autophagy contributes to the removal of protein aggregates. However, if and how proteotoxic stress induces autophagy is poorly understood. Here we show that proteotoxic stress after treatment with azetidine-2-carboxylic acid (AZC), a toxic proline analog, induces autophagy in budding yeast. AZC treatment attenuated target of rapamycin complex 1 (TORC1) activity, resulting in the dephosphorylation of Atg13, a key factor of autophagy. By contrast, AZC treatment did not affect target of rapamycin complex 2 (TORC2). Proteotoxic stress also induced TORC1 inactivation and autophagy in fission yeast and human cells. This study suggested that TORC1 is a conserved key factor to cope with proteotoxic stress in eukaryotic cells.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">30797551</PMID><DateCompleted><Year>2019</Year><Month>12</Month><Day>16</Day></DateCompleted><DateRevised><Year>2019</Year><Month>12</Month><Day>22</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1090-2104</ISSN><JournalIssue CitedMedium="Internet"><Volume>511</Volume><Issue>2</Issue><PubDate><Year>2019</Year><Month>04</Month><Day>02</Day></PubDate></JournalIssue><Title>Biochemical and biophysical research communications</Title><ISOAbbreviation>Biochem Biophys Res Commun</ISOAbbreviation></Journal><ArticleTitle>TORC1 regulates autophagy induction in response to proteotoxic stress in yeast and human cells.</ArticleTitle><Pagination><MedlinePgn>434-439</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0006-291X(19)30272-4</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.bbrc.2019.02.077</ELocationID><Abstract><AbstractText>Misfolded and aggregated proteins are eliminated to maintain protein homeostasis. Autophagy contributes to the removal of protein aggregates. However, if and how proteotoxic stress induces autophagy is poorly understood. Here we show that proteotoxic stress after treatment with azetidine-2-carboxylic acid (AZC), a toxic proline analog, induces autophagy in budding yeast. AZC treatment attenuated target of rapamycin complex 1 (TORC1) activity, resulting in the dephosphorylation of Atg13, a key factor of autophagy. By contrast, AZC treatment did not affect target of rapamycin complex 2 (TORC2). Proteotoxic stress also induced TORC1 inactivation and autophagy in fission yeast and human cells. This study suggested that TORC1 is a conserved key factor to cope with proteotoxic stress in eukaryotic cells.</AbstractText><CopyrightInformation>Copyright © 2019 Elsevier Inc. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Suda</LastName><ForeName>Kazuki</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Department of Biological Science, Shizuoka University, Shizuoka, 422-8021, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kaneko</LastName><ForeName>Atsuki</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Course of Biological Science, Department of Science, Graduate School of Integrated Science and Technology, Shizuoka University, Shizuoka, 422-8021, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Shimobayashi</LastName><ForeName>Mitsugu</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Biozentrum, University of Basel, 4056, Basel, Switzerland, Switzerland.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Nakashima</LastName><ForeName>Akio</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Biosignal Research Center, Kobe University, Kobe, 657-8501, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Maeda</LastName><ForeName>Tatsuya</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Department of Biology, Hamamatsu University School of Medicine, Hamamatsu, Shizuoka, 431-3192, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hall</LastName><ForeName>Michael N</ForeName><Initials>MN</Initials><AffiliationInfo><Affiliation>Biozentrum, University of Basel, 4056, Basel, Switzerland, Switzerland.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ushimaru</LastName><ForeName>Takashi</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Department of Biological Science, Shizuoka University, Shizuoka, 422-8021, Japan; Course of Biological Science, Department of Science, Graduate School of Integrated Science and Technology, Shizuoka University, Shizuoka, 422-8021, Japan. Electronic address: ushimaru.takashi@shizuoka.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>02</Month><Day>21</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Biochem Biophys Res Commun</MedlineTA><NlmUniqueID>0372516</NlmUniqueID><ISSNLinking>0006-291X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>5GZ3E0L9ZU</RegistryNumber><NameOfSubstance UI="D001383">Azetidinecarboxylic Acid</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber><NameOfSubstance UI="D000076222">Mechanistic Target of Rapamycin Complex 1</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001343" MajorTopicYN="N">Autophagy</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001383" MajorTopicYN="N">Azetidinecarboxylic Acid</DescriptorName><QualifierName UI="Q000633" MajorTopicYN="Y">toxicity</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D057809" MajorTopicYN="N">HEK293 Cells</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000076222" MajorTopicYN="N">Mechanistic Target of Rapamycin Complex 1</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000166" MajorTopicYN="N">cytology</QualifierName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012568" MajorTopicYN="N">Schizosaccharomyces</DescriptorName><QualifierName UI="Q000166" MajorTopicYN="N">cytology</QualifierName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">Autophagy</Keyword><Keyword MajorTopicYN="Y">Azetidine-2-carboxylic acid (AZC)</Keyword><Keyword MajorTopicYN="Y">Proteotoxic stress</Keyword><Keyword MajorTopicYN="Y">Target of rapamycin complex 1 (TORC1)</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2019</Year><Month>02</Month><Day>05</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2019</Year><Month>02</Month><Day>15</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2019</Year><Month>2</Month><Day>25</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2019</Year><Month>12</Month><Day>18</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2019</Year><Month>2</Month><Day>25</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">30797551</ArticleId><ArticleId IdType="pii">S0006-291X(19)30272-4</ArticleId><ArticleId IdType="doi">10.1016/j.bbrc.2019.02.077</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Japon</li><li>Suisse</li></country></list><tree><country name="Japon"><noRegion><name sortKey="Suda, Kazuki" sort="Suda, Kazuki" uniqKey="Suda K" first="Kazuki" last="Suda">Kazuki Suda</name></noRegion><name sortKey="Kaneko, Atsuki" sort="Kaneko, Atsuki" uniqKey="Kaneko A" first="Atsuki" last="Kaneko">Atsuki Kaneko</name><name sortKey="Maeda, Tatsuya" sort="Maeda, Tatsuya" uniqKey="Maeda T" first="Tatsuya" last="Maeda">Tatsuya Maeda</name><name sortKey="Nakashima, Akio" sort="Nakashima, Akio" uniqKey="Nakashima A" first="Akio" last="Nakashima">Akio Nakashima</name><name sortKey="Ushimaru, Takashi" sort="Ushimaru, Takashi" uniqKey="Ushimaru T" first="Takashi" last="Ushimaru">Takashi Ushimaru</name></country><country name="Suisse"><noRegion><name sortKey="Shimobayashi, Mitsugu" sort="Shimobayashi, Mitsugu" uniqKey="Shimobayashi M" first="Mitsugu" last="Shimobayashi">Mitsugu Shimobayashi</name></noRegion><name sortKey="Hall, Michael N" sort="Hall, Michael N" uniqKey="Hall M" first="Michael N" last="Hall">Michael N. 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