Sterol transporters at membrane contact sites regulate TORC1 and TORC2 signaling.
Identifieur interne : 000741 ( Main/Exploration ); précédent : 000740; suivant : 000742Sterol transporters at membrane contact sites regulate TORC1 and TORC2 signaling.
Auteurs : Andrew Murley [États-Unis] ; Justin Yamada [États-Unis] ; Bradley J. Niles [États-Unis] ; Alexandre Toulmay [États-Unis] ; William A. Prinz [États-Unis] ; Ted Powers [États-Unis] ; Jodi Nunnari [États-Unis]Source :
- The Journal of cell biology [ 1540-8140 ] ; 2017.
Descripteurs français
- KwdFr :
- Antiports (génétique), Antiports (métabolisme), Complexe-2 cible mécanistique de la rapamycine (MeSH), Complexes multiprotéiques (génétique), Complexes multiprotéiques (métabolisme), Facteurs de transcription (génétique), Facteurs de transcription (métabolisme), Microdomaines membranaires (enzymologie), Protéines de Saccharomyces cerevisiae (génétique), Protéines de Saccharomyces cerevisiae (métabolisme), Protéines de liaison à l'ARN (génétique), Protéines de liaison à l'ARN (métabolisme), Protéines de transport (génétique), Protéines de transport (métabolisme), Protéines du cytosquelette (MeSH), Réticulum endoplasmique (enzymologie), Saccharomyces cerevisiae (enzymologie), Saccharomyces cerevisiae (génétique), Stérols (métabolisme), Sérine-thréonine kinases TOR (génétique), Sérine-thréonine kinases TOR (métabolisme), Transduction du signal (MeSH), Transport biologique (MeSH), Vacuoles (enzymologie).
- MESH :
- enzymologie : Microdomaines membranaires, Réticulum endoplasmique, Saccharomyces cerevisiae, Vacuoles.
- génétique : Antiports, Complexes multiprotéiques, Facteurs de transcription, Protéines de Saccharomyces cerevisiae, Protéines de liaison à l'ARN, Protéines de transport, Saccharomyces cerevisiae, Sérine-thréonine kinases TOR.
- métabolisme : Antiports, Complexes multiprotéiques, Facteurs de transcription, Protéines de Saccharomyces cerevisiae, Protéines de liaison à l'ARN, Protéines de transport, Stérols, Sérine-thréonine kinases TOR.
- Complexe-2 cible mécanistique de la rapamycine, Protéines du cytosquelette, Transduction du signal, Transport biologique.
English descriptors
- KwdEn :
- Antiporters (genetics), Antiporters (metabolism), Biological Transport (MeSH), Carrier Proteins (genetics), Carrier Proteins (metabolism), Cytoskeletal Proteins (MeSH), Endoplasmic Reticulum (enzymology), Mechanistic Target of Rapamycin Complex 2 (MeSH), Membrane Microdomains (enzymology), Multiprotein Complexes (genetics), Multiprotein Complexes (metabolism), RNA-Binding Proteins (genetics), RNA-Binding Proteins (metabolism), Saccharomyces cerevisiae (enzymology), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism), Signal Transduction (MeSH), Sterols (metabolism), TOR Serine-Threonine Kinases (genetics), TOR Serine-Threonine Kinases (metabolism), Transcription Factors (genetics), Transcription Factors (metabolism), Vacuoles (enzymology).
- MESH :
- chemical , genetics : Antiporters, Carrier Proteins, Multiprotein Complexes, RNA-Binding Proteins, Saccharomyces cerevisiae Proteins, TOR Serine-Threonine Kinases, Transcription Factors.
- chemical , metabolism : Antiporters, Carrier Proteins, Multiprotein Complexes, RNA-Binding Proteins, Saccharomyces cerevisiae Proteins, Sterols, TOR Serine-Threonine Kinases, Transcription Factors.
- enzymology : Endoplasmic Reticulum, Membrane Microdomains, Saccharomyces cerevisiae, Vacuoles.
- genetics : Saccharomyces cerevisiae.
- Biological Transport, Cytoskeletal Proteins, Mechanistic Target of Rapamycin Complex 2, Signal Transduction.
Abstract
Membrane contact sites (MCSs) function to facilitate the formation of membrane domains composed of specialized lipids, proteins, and nucleic acids. In cells, membrane domains regulate membrane dynamics and biochemical and signaling pathways. We and others identified a highly conserved family of sterol transport proteins (Ltc/Lam) localized at diverse MCSs. In this study, we describe data indicating that the yeast family members Ltc1 and Ltc3/4 function at the vacuole and plasma membrane, respectively, to create membrane domains that partition upstream regulators of the TORC1 and TORC2 signaling pathways to coordinate cellular stress responses with sterol homeostasis.
DOI: 10.1083/jcb.201610032
PubMed: 28774891
PubMed Central: PMC5584152
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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(MeSH)</term><term>Endoplasmic Reticulum (enzymology)</term><term>Mechanistic Target of Rapamycin Complex 2 (MeSH)</term><term>Membrane Microdomains (enzymology)</term><term>Multiprotein Complexes (genetics)</term><term>Multiprotein Complexes (metabolism)</term><term>RNA-Binding Proteins (genetics)</term><term>RNA-Binding Proteins (metabolism)</term><term>Saccharomyces cerevisiae (enzymology)</term><term>Saccharomyces cerevisiae (genetics)</term><term>Saccharomyces cerevisiae Proteins (genetics)</term><term>Saccharomyces cerevisiae Proteins (metabolism)</term><term>Signal Transduction (MeSH)</term><term>Sterols (metabolism)</term><term>TOR Serine-Threonine Kinases (genetics)</term><term>TOR Serine-Threonine Kinases (metabolism)</term><term>Transcription Factors (genetics)</term><term>Transcription Factors (metabolism)</term><term>Vacuoles (enzymology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Antiports (génétique)</term><term>Antiports (métabolisme)</term><term>Complexe-2 cible mécanistique de la rapamycine (MeSH)</term><term>Complexes multiprotéiques (génétique)</term><term>Complexes multiprotéiques (métabolisme)</term><term>Facteurs de transcription (génétique)</term><term>Facteurs de transcription (métabolisme)</term><term>Microdomaines membranaires (enzymologie)</term><term>Protéines de Saccharomyces cerevisiae (génétique)</term><term>Protéines de Saccharomyces cerevisiae (métabolisme)</term><term>Protéines de liaison à l'ARN (génétique)</term><term>Protéines de liaison à l'ARN (métabolisme)</term><term>Protéines de transport (génétique)</term><term>Protéines de transport (métabolisme)</term><term>Protéines du cytosquelette (MeSH)</term><term>Réticulum endoplasmique (enzymologie)</term><term>Saccharomyces cerevisiae (enzymologie)</term><term>Saccharomyces cerevisiae (génétique)</term><term>Stérols (métabolisme)</term><term>Sérine-thréonine kinases TOR (génétique)</term><term>Sérine-thréonine kinases TOR (métabolisme)</term><term>Transduction du signal (MeSH)</term><term>Transport biologique (MeSH)</term><term>Vacuoles (enzymologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Antiporters</term><term>Carrier Proteins</term><term>Multiprotein Complexes</term><term>RNA-Binding Proteins</term><term>Saccharomyces cerevisiae Proteins</term><term>TOR Serine-Threonine Kinases</term><term>Transcription Factors</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Antiporters</term><term>Carrier Proteins</term><term>Multiprotein Complexes</term><term>RNA-Binding Proteins</term><term>Saccharomyces cerevisiae Proteins</term><term>Sterols</term><term>TOR Serine-Threonine Kinases</term><term>Transcription Factors</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Microdomaines membranaires</term><term>Réticulum endoplasmique</term><term>Saccharomyces cerevisiae</term><term>Vacuoles</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Endoplasmic Reticulum</term><term>Membrane Microdomains</term><term>Saccharomyces cerevisiae</term><term>Vacuoles</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Antiports</term><term>Complexes multiprotéiques</term><term>Facteurs de transcription</term><term>Protéines de Saccharomyces cerevisiae</term><term>Protéines de liaison à l'ARN</term><term>Protéines de transport</term><term>Saccharomyces cerevisiae</term><term>Sérine-thréonine kinases TOR</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Antiports</term><term>Complexes multiprotéiques</term><term>Facteurs de transcription</term><term>Protéines de Saccharomyces cerevisiae</term><term>Protéines de liaison à l'ARN</term><term>Protéines de transport</term><term>Stérols</term><term>Sérine-thréonine kinases TOR</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Biological Transport</term><term>Cytoskeletal Proteins</term><term>Mechanistic Target of Rapamycin Complex 2</term><term>Signal Transduction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Complexe-2 cible mécanistique de la rapamycine</term><term>Protéines du cytosquelette</term><term>Transduction du signal</term><term>Transport biologique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Membrane contact sites (MCSs) function to facilitate the formation of membrane domains composed of specialized lipids, proteins, and nucleic acids. In cells, membrane domains regulate membrane dynamics and biochemical and signaling pathways. We and others identified a highly conserved family of sterol transport proteins (Ltc/Lam) localized at diverse MCSs. In this study, we describe data indicating that the yeast family members Ltc1 and Ltc3/4 function at the vacuole and plasma membrane, respectively, to create membrane domains that partition upstream regulators of the TORC1 and TORC2 signaling pathways to coordinate cellular stress responses with sterol homeostasis.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">28774891</PMID><DateCompleted><Year>2017</Year><Month>10</Month><Day>04</Day></DateCompleted><DateRevised><Year>2019</Year><Month>12</Month><Day>10</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1540-8140</ISSN><JournalIssue CitedMedium="Internet"><Volume>216</Volume><Issue>9</Issue><PubDate><Year>2017</Year><Month>09</Month><Day>04</Day></PubDate></JournalIssue><Title>The Journal of cell biology</Title><ISOAbbreviation>J Cell Biol</ISOAbbreviation></Journal><ArticleTitle>Sterol transporters at membrane contact sites regulate TORC1 and TORC2 signaling.</ArticleTitle><Pagination><MedlinePgn>2679-2689</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1083/jcb.201610032</ELocationID><Abstract><AbstractText>Membrane contact sites (MCSs) function to facilitate the formation of membrane domains composed of specialized lipids, proteins, and nucleic acids. In cells, membrane domains regulate membrane dynamics and biochemical and signaling pathways. We and others identified a highly conserved family of sterol transport proteins (Ltc/Lam) localized at diverse MCSs. In this study, we describe data indicating that the yeast family members Ltc1 and Ltc3/4 function at the vacuole and plasma membrane, respectively, to create membrane domains that partition upstream regulators of the TORC1 and TORC2 signaling pathways to coordinate cellular stress responses with sterol homeostasis.</AbstractText><CopyrightInformation>© 2017 Murley et al.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Murley</LastName><ForeName>Andrew</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Department of Molecular and Cellular Biology, University of California, Davis, Davis, CA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yamada</LastName><ForeName>Justin</ForeName><Initials>J</Initials><Identifier Source="ORCID">0000-0003-1933-3721</Identifier><AffiliationInfo><Affiliation>Department of Molecular and Cellular Biology, University of California, Davis, Davis, CA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Niles</LastName><ForeName>Bradley J</ForeName><Initials>BJ</Initials><AffiliationInfo><Affiliation>Department of Molecular and Cellular Biology, University of California, Davis, Davis, CA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Toulmay</LastName><ForeName>Alexandre</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Prinz</LastName><ForeName>William A</ForeName><Initials>WA</Initials><Identifier Source="ORCID">0000-0002-9053-2398</Identifier><AffiliationInfo><Affiliation>National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Powers</LastName><ForeName>Ted</ForeName><Initials>T</Initials><Identifier Source="ORCID">0000-0002-2007-3819</Identifier><AffiliationInfo><Affiliation>Department of Molecular and Cellular Biology, University of California, Davis, Davis, CA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Nunnari</LastName><ForeName>Jodi</ForeName><Initials>J</Initials><Identifier Source="ORCID">0000-0002-2249-8730</Identifier><AffiliationInfo><Affiliation>Department of Molecular and Cellular Biology, University of California, Davis, Davis, CA jmnunnari@ucdavis.edu.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>T32 GM007377</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2017</Year><Month>08</Month><Day>03</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Cell Biol</MedlineTA><NlmUniqueID>0375356</NlmUniqueID><ISSNLinking>0021-9525</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D017920">Antiporters</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D002352">Carrier Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D003598">Cytoskeletal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C000599842">LTC1 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D046912">Multiprotein Complexes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D016601">RNA-Binding Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029701">Saccharomyces cerevisiae Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C502930">Slm1 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C502931">Slm2 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D013261">Sterols</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>EC 2.7.1.1</RegistryNumber><NameOfSubstance UI="D058570">TOR Serine-Threonine Kinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber><NameOfSubstance UI="D000076225">Mechanistic Target of Rapamycin Complex 2</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D017920" MajorTopicYN="N">Antiporters</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001692" MajorTopicYN="N">Biological Transport</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002352" MajorTopicYN="N">Carrier Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003598" MajorTopicYN="N">Cytoskeletal Proteins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004721" MajorTopicYN="N">Endoplasmic Reticulum</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000076225" MajorTopicYN="N">Mechanistic Target of Rapamycin Complex 2</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D021962" MajorTopicYN="N">Membrane Microdomains</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D046912" MajorTopicYN="N">Multiprotein Complexes</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016601" MajorTopicYN="N">RNA-Binding Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029701" MajorTopicYN="N">Saccharomyces cerevisiae Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015398" MajorTopicYN="N">Signal Transduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013261" MajorTopicYN="N">Sterols</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D058570" MajorTopicYN="N">TOR Serine-Threonine Kinases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" 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Niles</name><name sortKey="Nunnari, Jodi" sort="Nunnari, Jodi" uniqKey="Nunnari J" first="Jodi" last="Nunnari">Jodi Nunnari</name><name sortKey="Powers, Ted" sort="Powers, Ted" uniqKey="Powers T" first="Ted" last="Powers">Ted Powers</name><name sortKey="Prinz, William A" sort="Prinz, William A" uniqKey="Prinz W" first="William A" last="Prinz">William A. Prinz</name><name sortKey="Toulmay, Alexandre" sort="Toulmay, Alexandre" uniqKey="Toulmay A" first="Alexandre" last="Toulmay">Alexandre Toulmay</name><name sortKey="Yamada, Justin" sort="Yamada, Justin" uniqKey="Yamada J" first="Justin" last="Yamada">Justin Yamada</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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