Multilayered regulation of TORC1-body formation in budding yeast.
Identifieur interne : 000273 ( Main/Exploration ); précédent : 000272; suivant : 000274Multilayered regulation of TORC1-body formation in budding yeast.
Auteurs : Arron Sullivan [États-Unis] ; Ryan L. Wallace [États-Unis] ; Rachel Wellington [États-Unis] ; Xiangxia Luo [États-Unis] ; Andrew P. Capaldi [États-Unis]Source :
- Molecular biology of the cell [ 1939-4586 ] ; 2019.
Descripteurs français
- KwdFr :
- MESH :
- composition chimique : Protéines de Saccharomyces cerevisiae.
- métabolisme : Complexe-1 cible mécanistique de la rapamycine, Protéines de Saccharomyces cerevisiae, Saccharomycetales.
- Domaines protéiques, Modèles biologiques.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Saccharomyces cerevisiae Proteins.
- chemical , metabolism : Mechanistic Target of Rapamycin Complex 1, Saccharomyces cerevisiae Proteins.
- metabolism : Saccharomycetales.
- Models, Biological, Protein Domains.
Abstract
The target of rapamycin kinase complex 1 (TORC1) regulates cell growth and metabolism in eukaryotes. In Saccharomyces cerevisiae, TORC1 activity is known to be controlled by the conserved GTPases, Gtr1/2, and movement into and out of an inactive agglomerate/body. However, it is unclear whether/how these regulatory steps are coupled. Here we show that active Gtr1/2 is a potent inhibitor of TORC1-body formation, but cells missing Gtr1/2 still form TORC1-bodies in a glucose/nitrogen starvation-dependent manner. We also identify 13 new activators of TORC1-body formation and show that seven of these proteins regulate the Gtr1/2-dependent repression of TORC1-body formation, while the remaining proteins drive the subsequent steps in TORC1 agglomeration. Finally, we show that the conserved phosphatidylinositol-3-phosphate (PI(3)P) binding protein, Pib2, forms a complex with TORC1 and overrides the Gtr1/2-dependent repression of TORC1-body formation during starvation. These data provide a unified, systems-level model of TORC1 regulation in yeast.
DOI: 10.1091/mbc.E18-05-0297
PubMed: 30485160
PubMed Central: PMC6589571
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Capaldi</name><affiliation wicri:level="2"><nlm:affiliation>Department of Molecular and Cellular Biology, University of Arizona, Tucson, AZ 85721-0206.</nlm:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Arizona</region></placeName><wicri:cityArea>Department of Molecular and Cellular Biology, University of Arizona, Tucson</wicri:cityArea></affiliation></author></analytic><series><title level="j">Molecular biology of the cell</title><idno type="eISSN">1939-4586</idno><imprint><date when="2019" type="published">2019</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Mechanistic Target of Rapamycin Complex 1 (metabolism)</term><term>Models, Biological (MeSH)</term><term>Protein Domains (MeSH)</term><term>Saccharomyces cerevisiae Proteins (chemistry)</term><term>Saccharomyces cerevisiae Proteins (metabolism)</term><term>Saccharomycetales (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Complexe-1 cible mécanistique de la rapamycine (métabolisme)</term><term>Domaines protéiques (MeSH)</term><term>Modèles biologiques (MeSH)</term><term>Protéines de Saccharomyces cerevisiae (composition chimique)</term><term>Protéines de Saccharomyces cerevisiae (métabolisme)</term><term>Saccharomycetales (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Saccharomyces cerevisiae Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Mechanistic Target of Rapamycin Complex 1</term><term>Saccharomyces cerevisiae Proteins</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Protéines de Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Saccharomycetales</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Complexe-1 cible mécanistique de la rapamycine</term><term>Protéines de Saccharomyces cerevisiae</term><term>Saccharomycetales</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Models, Biological</term><term>Protein Domains</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Domaines protéiques</term><term>Modèles biologiques</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The target of rapamycin kinase complex 1 (TORC1) regulates cell growth and metabolism in eukaryotes. In Saccharomyces cerevisiae, TORC1 activity is known to be controlled by the conserved GTPases, Gtr1/2, and movement into and out of an inactive agglomerate/body. However, it is unclear whether/how these regulatory steps are coupled. Here we show that active Gtr1/2 is a potent inhibitor of TORC1-body formation, but cells missing Gtr1/2 still form TORC1-bodies in a glucose/nitrogen starvation-dependent manner. We also identify 13 new activators of TORC1-body formation and show that seven of these proteins regulate the Gtr1/2-dependent repression of TORC1-body formation, while the remaining proteins drive the subsequent steps in TORC1 agglomeration. Finally, we show that the conserved phosphatidylinositol-3-phosphate (PI(3)P) binding protein, Pib2, forms a complex with TORC1 and overrides the Gtr1/2-dependent repression of TORC1-body formation during starvation. These data provide a unified, systems-level model of TORC1 regulation in yeast.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">30485160</PMID><DateCompleted><Year>2019</Year><Month>06</Month><Day>25</Day></DateCompleted><DateRevised><Year>2020</Year><Month>02</Month><Day>25</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1939-4586</ISSN><JournalIssue CitedMedium="Internet"><Volume>30</Volume><Issue>3</Issue><PubDate><Year>2019</Year><Month>02</Month><Day>01</Day></PubDate></JournalIssue><Title>Molecular biology of the cell</Title><ISOAbbreviation>Mol Biol Cell</ISOAbbreviation></Journal><ArticleTitle>Multilayered regulation of TORC1-body formation in budding yeast.</ArticleTitle><Pagination><MedlinePgn>400-410</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1091/mbc.E18-05-0297</ELocationID><Abstract><AbstractText>The target of rapamycin kinase complex 1 (TORC1) regulates cell growth and metabolism in eukaryotes. In Saccharomyces cerevisiae, TORC1 activity is known to be controlled by the conserved GTPases, Gtr1/2, and movement into and out of an inactive agglomerate/body. However, it is unclear whether/how these regulatory steps are coupled. Here we show that active Gtr1/2 is a potent inhibitor of TORC1-body formation, but cells missing Gtr1/2 still form TORC1-bodies in a glucose/nitrogen starvation-dependent manner. We also identify 13 new activators of TORC1-body formation and show that seven of these proteins regulate the Gtr1/2-dependent repression of TORC1-body formation, while the remaining proteins drive the subsequent steps in TORC1 agglomeration. Finally, we show that the conserved phosphatidylinositol-3-phosphate (PI(3)P) binding protein, Pib2, forms a complex with TORC1 and overrides the Gtr1/2-dependent repression of TORC1-body formation during starvation. These data provide a unified, systems-level model of TORC1 regulation in yeast.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Sullivan</LastName><ForeName>Arron</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Department of Molecular and Cellular Biology, University of Arizona, Tucson, AZ 85721-0206.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wallace</LastName><ForeName>Ryan L</ForeName><Initials>RL</Initials><AffiliationInfo><Affiliation>Department of Molecular and Cellular Biology, University of Arizona, Tucson, AZ 85721-0206.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wellington</LastName><ForeName>Rachel</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Department of Molecular and Cellular Biology, University of Arizona, Tucson, AZ 85721-0206.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Luo</LastName><ForeName>Xiangxia</ForeName><Initials>X</Initials><AffiliationInfo><Affiliation>Department of Molecular and Cellular Biology, University of Arizona, Tucson, AZ 85721-0206.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Capaldi</LastName><ForeName>Andrew P</ForeName><Initials>AP</Initials><AffiliationInfo><Affiliation>Department of Molecular and Cellular Biology, University of Arizona, Tucson, AZ 85721-0206.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01 GM097329</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>T32 GM008659</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., 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Capaldi</name><name sortKey="Luo, Xiangxia" sort="Luo, Xiangxia" uniqKey="Luo X" first="Xiangxia" last="Luo">Xiangxia Luo</name><name sortKey="Wallace, Ryan L" sort="Wallace, Ryan L" uniqKey="Wallace R" first="Ryan L" last="Wallace">Ryan L. Wallace</name><name sortKey="Wellington, Rachel" sort="Wellington, Rachel" uniqKey="Wellington R" first="Rachel" last="Wellington">Rachel Wellington</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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