The Rag GTPase-Ragulator complex attenuates TOR complex 1 signaling in fission yeast.
Identifieur interne : 000459 ( Main/Exploration ); précédent : 000458; suivant : 000460The Rag GTPase-Ragulator complex attenuates TOR complex 1 signaling in fission yeast.
Auteurs : Tomoyuki Fukuda [Japon] ; Kazuhiro Shiozaki [Japon, États-Unis]Source :
- Autophagy [ 1554-8635 ] ; 2018.
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Abstract
Target of rapamycin complex 1 (TORC1) is an evolutionarily conserved protein kinase complex, whose activation in response to nutrients suppresses autophagy. In mammalian cells, amino-acid stimuli induce lysosomal translocation and activation of MTORC1 through the RRAG GTPase heterodimer, which is tethered to the surface of lysosomes by the Ragulator complex. Our recent study demonstrated that the fission yeast Schizosaccharomyces pombe also has a Ragulator complex that anchors the Gtr1-Gtr2 Rag GTPase heterodimer to the vacuole, a lysosome-like organelle. Unexpectedly, however, neither vacuolar localization nor activation of TORC1 is dependent on the Rag-Ragulator complex, which instead plays a critical role in attenuating TORC1 signaling. Our findings suggest dual functionality of the Rag GTPase in both activation and inactivation of TORC1.
DOI: 10.1080/15548627.2018.1444313
PubMed: 29799770
PubMed Central: PMC6103401
Affiliations:
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School of Medical and Dental Sciences , Niigata </wicri:regionArea><wicri:noRegion>Niigata </wicri:noRegion></affiliation></author><author><name sortKey="Shiozaki, Kazuhiro" sort="Shiozaki, Kazuhiro" uniqKey="Shiozaki K" first="Kazuhiro" last="Shiozaki">Kazuhiro Shiozaki</name><affiliation wicri:level="1"><nlm:affiliation>a Graduate School of Biological Sciences , Nara Institute of Science and Technology , Ikoma , Nara , Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>a Graduate School of Biological Sciences , Nara Institute of Science and Technology , Ikoma , Nara </wicri:regionArea><wicri:noRegion>Nara </wicri:noRegion></affiliation><affiliation wicri:level="2"><nlm:affiliation>c Department of Microbiology and Molecular Genetics , University of California , Davis , CA USA.</nlm:affiliation><country>États-Unis</country><placeName><region type="state">Californie</region></placeName><wicri:cityArea>c Department of Microbiology and Molecular Genetics , 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wicri:level="1"><nlm:affiliation>a Graduate School of Biological Sciences , Nara Institute of Science and Technology , Ikoma , Nara , Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>a Graduate School of Biological Sciences , Nara Institute of Science and Technology , Ikoma , Nara </wicri:regionArea><wicri:noRegion>Nara </wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:affiliation>b Department of Cellular Physiology , Niigata University Graduate School of Medical and Dental Sciences , Niigata , Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>b Department of Cellular Physiology , Niigata University Graduate School of Medical and Dental Sciences , Niigata </wicri:regionArea><wicri:noRegion>Niigata </wicri:noRegion></affiliation></author><author><name sortKey="Shiozaki, Kazuhiro" sort="Shiozaki, Kazuhiro" uniqKey="Shiozaki K" first="Kazuhiro" last="Shiozaki">Kazuhiro Shiozaki</name><affiliation wicri:level="1"><nlm:affiliation>a Graduate School of Biological Sciences , Nara Institute of Science and Technology , Ikoma , Nara , Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>a Graduate School of Biological Sciences , Nara Institute of Science and Technology , Ikoma , Nara </wicri:regionArea><wicri:noRegion>Nara </wicri:noRegion></affiliation><affiliation wicri:level="2"><nlm:affiliation>c Department of Microbiology and Molecular Genetics , University of California , Davis , CA USA.</nlm:affiliation><country>États-Unis</country><placeName><region type="state">Californie</region></placeName><wicri:cityArea>c Department of Microbiology and Molecular Genetics , University of California , Davis </wicri:cityArea></affiliation></author></analytic><series><title level="j">Autophagy</title><idno type="eISSN">1554-8635</idno><imprint><date when="2018" type="published">2018</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term><term>Autophagy (MeSH)</term><term>Lysosomes (MeSH)</term><term>Mechanistic Target of Rapamycin Complex 1 (MeSH)</term><term>Monomeric GTP-Binding Proteins (MeSH)</term><term>Schizosaccharomyces (MeSH)</term><term>Signal Transduction (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Autophagie (MeSH)</term><term>Complexe-1 cible mécanistique de la rapamycine (MeSH)</term><term>Lysosomes (MeSH)</term><term>Protéines G monomériques (MeSH)</term><term>Schizosaccharomyces (MeSH)</term><term>Transduction du signal (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Mechanistic Target of Rapamycin Complex 1</term><term>Monomeric GTP-Binding Proteins</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Autophagy</term><term>Lysosomes</term><term>Schizosaccharomyces</term><term>Signal Transduction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Autophagie</term><term>Complexe-1 cible mécanistique de la rapamycine</term><term>Lysosomes</term><term>Protéines G monomériques</term><term>Schizosaccharomyces</term><term>Transduction du signal</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Target of rapamycin complex 1 (TORC1) is an evolutionarily conserved protein kinase complex, whose activation in response to nutrients suppresses autophagy. In mammalian cells, amino-acid stimuli induce lysosomal translocation and activation of MTORC1 through the RRAG GTPase heterodimer, which is tethered to the surface of lysosomes by the Ragulator complex. Our recent study demonstrated that the fission yeast Schizosaccharomyces pombe also has a Ragulator complex that anchors the Gtr1-Gtr2 Rag GTPase heterodimer to the vacuole, a lysosome-like organelle. Unexpectedly, however, neither vacuolar localization nor activation of TORC1 is dependent on the Rag-Ragulator complex, which instead plays a critical role in attenuating TORC1 signaling. Our findings suggest dual functionality of the Rag GTPase in both activation and inactivation of TORC1.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" IndexingMethod="Automated" Owner="NLM"><PMID Version="1">29799770</PMID><DateCompleted><Year>2019</Year><Month>06</Month><Day>28</Day></DateCompleted><DateRevised><Year>2019</Year><Month>06</Month><Day>28</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1554-8635</ISSN><JournalIssue CitedMedium="Internet"><Volume>14</Volume><Issue>6</Issue><PubDate><Year>2018</Year></PubDate></JournalIssue><Title>Autophagy</Title><ISOAbbreviation>Autophagy</ISOAbbreviation></Journal><ArticleTitle>The Rag GTPase-Ragulator complex attenuates TOR complex 1 signaling in fission yeast.</ArticleTitle><Pagination><MedlinePgn>1105-1106</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1080/15548627.2018.1444313</ELocationID><Abstract><AbstractText>Target of rapamycin complex 1 (TORC1) is an evolutionarily conserved protein kinase complex, whose activation in response to nutrients suppresses autophagy. In mammalian cells, amino-acid stimuli induce lysosomal translocation and activation of MTORC1 through the RRAG GTPase heterodimer, which is tethered to the surface of lysosomes by the Ragulator complex. Our recent study demonstrated that the fission yeast Schizosaccharomyces pombe also has a Ragulator complex that anchors the Gtr1-Gtr2 Rag GTPase heterodimer to the vacuole, a lysosome-like organelle. Unexpectedly, however, neither vacuolar localization nor activation of TORC1 is dependent on the Rag-Ragulator complex, which instead plays a critical role in attenuating TORC1 signaling. Our findings suggest dual functionality of the Rag GTPase in both activation and inactivation of TORC1.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Fukuda</LastName><ForeName>Tomoyuki</ForeName><Initials>T</Initials><Identifier Source="ORCID">0000-0003-2069-7127</Identifier><AffiliationInfo><Affiliation>a Graduate School of Biological Sciences , Nara Institute of Science and Technology , Ikoma , Nara , Japan.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>b Department of Cellular Physiology , Niigata University Graduate School of Medical and Dental Sciences , Niigata , Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Shiozaki</LastName><ForeName>Kazuhiro</ForeName><Initials>K</Initials><Identifier Source="ORCID">0000-0002-0395-5457</Identifier><AffiliationInfo><Affiliation>a Graduate School of Biological Sciences , Nara Institute of Science and Technology , Ikoma , Nara , Japan.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>c Department of Microbiology and Molecular Genetics , University of California , Davis , CA USA.</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><PublicationType UI="D016420">Comment</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2018</Year><Month>05</Month><Day>25</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Autophagy</MedlineTA><NlmUniqueID>101265188</NlmUniqueID><ISSNLinking>1554-8627</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber><NameOfSubstance UI="D000076222">Mechanistic Target of Rapamycin Complex 1</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.6.5.2</RegistryNumber><NameOfSubstance UI="D020559">Monomeric GTP-Binding Proteins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><CommentsCorrectionsList><CommentsCorrections RefType="CommentOn"><RefSource>Elife. 2017 Dec 04;6:</RefSource><PMID Version="1">29199950</PMID></CommentsCorrections></CommentsCorrectionsList><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001343" MajorTopicYN="Y">Autophagy</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008247" MajorTopicYN="N">Lysosomes</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000076222" MajorTopicYN="N">Mechanistic Target of Rapamycin Complex 1</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020559" MajorTopicYN="Y">Monomeric GTP-Binding Proteins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012568" MajorTopicYN="Y">Schizosaccharomyces</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015398" MajorTopicYN="N">Signal Transduction</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">GATOR1</Keyword><Keyword MajorTopicYN="Y">Rag GTPase</Keyword><Keyword MajorTopicYN="Y">Ragulator</Keyword><Keyword MajorTopicYN="Y">TOR</Keyword><Keyword MajorTopicYN="Y">TORC1</Keyword><Keyword MajorTopicYN="Y">autophagy</Keyword><Keyword MajorTopicYN="Y">proliferation</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2018</Year><Month>5</Month><Day>26</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2019</Year><Month>6</Month><Day>30</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2018</Year><Month>5</Month><Day>26</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">29799770</ArticleId><ArticleId IdType="doi">10.1080/15548627.2018.1444313</ArticleId><ArticleId IdType="pmc">PMC6103401</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Japon</li><li>États-Unis</li></country><region><li>Californie</li></region></list><tree><country name="Japon"><noRegion><name sortKey="Fukuda, Tomoyuki" sort="Fukuda, Tomoyuki" uniqKey="Fukuda T" first="Tomoyuki" last="Fukuda">Tomoyuki Fukuda</name></noRegion><name sortKey="Fukuda, Tomoyuki" sort="Fukuda, Tomoyuki" uniqKey="Fukuda T" first="Tomoyuki" last="Fukuda">Tomoyuki Fukuda</name><name sortKey="Shiozaki, Kazuhiro" sort="Shiozaki, Kazuhiro" uniqKey="Shiozaki K" first="Kazuhiro" last="Shiozaki">Kazuhiro Shiozaki</name></country><country name="États-Unis"><region name="Californie"><name sortKey="Shiozaki, Kazuhiro" sort="Shiozaki, Kazuhiro" uniqKey="Shiozaki K" first="Kazuhiro" last="Shiozaki">Kazuhiro Shiozaki</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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