Analysis of the roles of phosphatidylinositol-4,5-bisphosphate and individual subunits in assembly, localization, and function of Saccharomyces cerevisiae target of rapamycin complex 2.
Identifieur interne : 000390 ( Main/Exploration ); précédent : 000389; suivant : 000391Analysis of the roles of phosphatidylinositol-4,5-bisphosphate and individual subunits in assembly, localization, and function of Saccharomyces cerevisiae target of rapamycin complex 2.
Auteurs : Maria Nieves Martinez Marshall [États-Unis] ; Anita Emmerstorfer-Augustin [États-Unis] ; Kristin L. Leskoske [États-Unis] ; Lydia H. Zhang [États-Unis] ; Biyun Li [États-Unis] ; Jeremy Thorner [États-Unis]Source :
- Molecular biology of the cell [ 1939-4586 ] ; 2019.
Descripteurs français
- KwdFr :
- Complexe-2 cible mécanistique de la rapamycine (métabolisme), Domaines protéiques (MeSH), Membrane cellulaire (métabolisme), Phosphatidylinositol diphosphate-4,5 (métabolisme), Protéines de Saccharomyces cerevisiae (composition chimique), Protéines de Saccharomyces cerevisiae (métabolisme), Protéines de transport (composition chimique), Protéines de transport (métabolisme), Protéines à domaine armadillo (composition chimique), Protéines à domaine armadillo (métabolisme), Saccharomyces cerevisiae (métabolisme), Sous-unités de protéines (métabolisme).
- MESH :
- composition chimique : Protéines de Saccharomyces cerevisiae, Protéines de transport, Protéines à domaine armadillo.
- métabolisme : Complexe-2 cible mécanistique de la rapamycine, Membrane cellulaire, Phosphatidylinositol diphosphate-4,5, Protéines de Saccharomyces cerevisiae, Protéines de transport, Protéines à domaine armadillo, Saccharomyces cerevisiae, Sous-unités de protéines.
- Domaines protéiques.
English descriptors
- KwdEn :
- Armadillo Domain Proteins (chemistry), Armadillo Domain Proteins (metabolism), Carrier Proteins (chemistry), Carrier Proteins (metabolism), Cell Membrane (metabolism), Mechanistic Target of Rapamycin Complex 2 (metabolism), Phosphatidylinositol 4,5-Diphosphate (metabolism), Protein Domains (MeSH), Protein Subunits (metabolism), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (chemistry), Saccharomyces cerevisiae Proteins (metabolism).
- MESH :
- chemical , chemistry : Armadillo Domain Proteins, Carrier Proteins, Saccharomyces cerevisiae Proteins.
- chemical , metabolism : Armadillo Domain Proteins, Carrier Proteins, Mechanistic Target of Rapamycin Complex 2, Phosphatidylinositol 4,5-Diphosphate, Protein Subunits, Saccharomyces cerevisiae Proteins.
- metabolism : Cell Membrane, Saccharomyces cerevisiae.
- Protein Domains.
Abstract
Eukaryotic cell survival requires maintenance of plasma membrane (PM) homeostasis in response to environmental insults and changes in lipid metabolism. In yeast, a key regulator of PM homeostasis is target of rapamycin (TOR) complex 2 (TORC2), a multiprotein complex containing the evolutionarily conserved TOR protein kinase isoform Tor2. PM localization is essential for TORC2 function. One core TORC2 subunit (Avo1) and two TORC2--associated regulators (Slm1 and Slm2) contain pleckstrin homology (PH) domains that exhibit specificity for binding phosphatidylinositol-4,5-bisphosphate (PtdIns4,5P2). To investigate the roles of PtdIns4,5P2 and constituent subunits of TORC2, we used auxin-inducible degradation to systematically eliminate these factors and then examined localization, association, and function of the remaining TORC2 components. We found that PtdIns4,5P2 depletion significantly reduced TORC2 activity, yet did not prevent PM localization or disassembly of TORC2. Moreover, truncated Avo1 (lacking its C-terminal PH domain) was still recruited to the PM and supported growth. Even when all three PH-containing proteins were absent, the remaining TORC2 subunits were PM-bound. Revealingly, Avo3 localized to the PM independent of both Avo1 and Tor2, whereas both Tor2 and Avo1 required Avo3 for their PM anchoring. Our findings provide new mechanistic information about TORC2 and pinpoint Avo3 as pivotal for TORC2 PM localization and assembly in vivo.
DOI: 10.1091/mbc.E18-10-0682
PubMed: 30969890
PubMed Central: PMC6724684
Affiliations:
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Leskoske</name><affiliation wicri:level="2"><nlm:affiliation>Division of Biochemistry, Biophysics and Structural Biology, Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720.</nlm:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Californie</region></placeName><wicri:cityArea>Division of Biochemistry, Biophysics and Structural Biology, Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley</wicri:cityArea></affiliation></author><author><name sortKey="Zhang, Lydia H" sort="Zhang, Lydia H" uniqKey="Zhang L" first="Lydia H" last="Zhang">Lydia H. Zhang</name><affiliation wicri:level="2"><nlm:affiliation>Division of Biochemistry, Biophysics and Structural Biology, Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720.</nlm:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Californie</region></placeName><wicri:cityArea>Division of Biochemistry, Biophysics and Structural Biology, Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley</wicri:cityArea></affiliation></author><author><name sortKey="Li, Biyun" sort="Li, Biyun" uniqKey="Li B" first="Biyun" last="Li">Biyun Li</name><affiliation wicri:level="2"><nlm:affiliation>Division of Biochemistry, Biophysics and Structural Biology, Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720.</nlm:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Californie</region></placeName><wicri:cityArea>Division of Biochemistry, Biophysics and Structural Biology, Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley</wicri:cityArea></affiliation></author><author><name sortKey="Thorner, Jeremy" sort="Thorner, Jeremy" uniqKey="Thorner J" first="Jeremy" last="Thorner">Jeremy Thorner</name><affiliation wicri:level="2"><nlm:affiliation>Division of Biochemistry, Biophysics and Structural Biology, Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720.</nlm:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Californie</region></placeName><wicri:cityArea>Division of Biochemistry, Biophysics and Structural Biology, Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley</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>Armadillo Domain Proteins (chemistry)</term><term>Armadillo Domain Proteins (metabolism)</term><term>Carrier Proteins (chemistry)</term><term>Carrier Proteins (metabolism)</term><term>Cell Membrane (metabolism)</term><term>Mechanistic Target of Rapamycin Complex 2 (metabolism)</term><term>Phosphatidylinositol 4,5-Diphosphate (metabolism)</term><term>Protein Domains (MeSH)</term><term>Protein Subunits (metabolism)</term><term>Saccharomyces cerevisiae (metabolism)</term><term>Saccharomyces cerevisiae Proteins (chemistry)</term><term>Saccharomyces cerevisiae Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Complexe-2 cible mécanistique de la rapamycine (métabolisme)</term><term>Domaines protéiques (MeSH)</term><term>Membrane cellulaire (métabolisme)</term><term>Phosphatidylinositol diphosphate-4,5 (métabolisme)</term><term>Protéines de Saccharomyces cerevisiae (composition chimique)</term><term>Protéines de Saccharomyces cerevisiae (métabolisme)</term><term>Protéines de transport (composition chimique)</term><term>Protéines de transport (métabolisme)</term><term>Protéines à domaine armadillo (composition chimique)</term><term>Protéines à domaine armadillo (métabolisme)</term><term>Saccharomyces cerevisiae (métabolisme)</term><term>Sous-unités de protéines (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Armadillo Domain Proteins</term><term>Carrier Proteins</term><term>Saccharomyces cerevisiae Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Armadillo Domain Proteins</term><term>Carrier Proteins</term><term>Mechanistic Target of Rapamycin Complex 2</term><term>Phosphatidylinositol 4,5-Diphosphate</term><term>Protein Subunits</term><term>Saccharomyces cerevisiae Proteins</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Protéines de Saccharomyces cerevisiae</term><term>Protéines de transport</term><term>Protéines à domaine armadillo</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cell Membrane</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Complexe-2 cible mécanistique de la rapamycine</term><term>Membrane cellulaire</term><term>Phosphatidylinositol diphosphate-4,5</term><term>Protéines de Saccharomyces cerevisiae</term><term>Protéines de transport</term><term>Protéines à domaine armadillo</term><term>Saccharomyces cerevisiae</term><term>Sous-unités de protéines</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Protein Domains</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Domaines protéiques</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Eukaryotic cell survival requires maintenance of plasma membrane (PM) homeostasis in response to environmental insults and changes in lipid metabolism. In yeast, a key regulator of PM homeostasis is target of rapamycin (TOR) complex 2 (TORC2), a multiprotein complex containing the evolutionarily conserved TOR protein kinase isoform Tor2. PM localization is essential for TORC2 function. One core TORC2 subunit (Avo1) and two TORC2--associated regulators (Slm1 and Slm2) contain pleckstrin homology (PH) domains that exhibit specificity for binding phosphatidylinositol-4,5-<i>bis</i>phosphate (PtdIns4,5P2). To investigate the roles of PtdIns4,5P2 and constituent subunits of TORC2, we used auxin-inducible degradation to systematically eliminate these factors and then examined localization, association, and function of the remaining TORC2 components. We found that PtdIns4,5P2 depletion significantly reduced TORC2 activity, yet did not prevent PM localization or disassembly of TORC2. Moreover, truncated Avo1 (lacking its C-terminal PH domain) was still recruited to the PM and supported growth. Even when all three PH-containing proteins were absent, the remaining TORC2 subunits were PM-bound. Revealingly, Avo3 localized to the PM independent of both Avo1 and Tor2, whereas both Tor2 and Avo1 required Avo3 for their PM anchoring. Our findings provide new mechanistic information about TORC2 and pinpoint Avo3 as pivotal for TORC2 PM localization and assembly in vivo.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">30969890</PMID><DateCompleted><Year>2020</Year><Month>01</Month><Day>08</Day></DateCompleted><DateRevised><Year>2020</Year><Month>03</Month><Day>09</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1939-4586</ISSN><JournalIssue CitedMedium="Internet"><Volume>30</Volume><Issue>12</Issue><PubDate><Year>2019</Year><Month>06</Month><Day>01</Day></PubDate></JournalIssue><Title>Molecular biology of the cell</Title><ISOAbbreviation>Mol Biol Cell</ISOAbbreviation></Journal><ArticleTitle>Analysis of the roles of phosphatidylinositol-4,5-<i>bis</i>phosphate and individual subunits in assembly, localization, and function of <i>Saccharomyces cerevisiae</i> target of rapamycin complex 2.</ArticleTitle><Pagination><MedlinePgn>1555-1574</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1091/mbc.E18-10-0682</ELocationID><Abstract><AbstractText>Eukaryotic cell survival requires maintenance of plasma membrane (PM) homeostasis in response to environmental insults and changes in lipid metabolism. In yeast, a key regulator of PM homeostasis is target of rapamycin (TOR) complex 2 (TORC2), a multiprotein complex containing the evolutionarily conserved TOR protein kinase isoform Tor2. PM localization is essential for TORC2 function. One core TORC2 subunit (Avo1) and two TORC2--associated regulators (Slm1 and Slm2) contain pleckstrin homology (PH) domains that exhibit specificity for binding phosphatidylinositol-4,5-<i>bis</i>phosphate (PtdIns4,5P2). To investigate the roles of PtdIns4,5P2 and constituent subunits of TORC2, we used auxin-inducible degradation to systematically eliminate these factors and then examined localization, association, and function of the remaining TORC2 components. We found that PtdIns4,5P2 depletion significantly reduced TORC2 activity, yet did not prevent PM localization or disassembly of TORC2. Moreover, truncated Avo1 (lacking its C-terminal PH domain) was still recruited to the PM and supported growth. Even when all three PH-containing proteins were absent, the remaining TORC2 subunits were PM-bound. Revealingly, Avo3 localized to the PM independent of both Avo1 and Tor2, whereas both Tor2 and Avo1 required Avo3 for their PM anchoring. Our findings provide new mechanistic information about TORC2 and pinpoint Avo3 as pivotal for TORC2 PM localization and assembly in vivo.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Martinez Marshall</LastName><ForeName>Maria Nieves</ForeName><Initials>MN</Initials><AffiliationInfo><Affiliation>Division of Biochemistry, Biophysics and Structural Biology, Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Emmerstorfer-Augustin</LastName><ForeName>Anita</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Division of Biochemistry, Biophysics and Structural Biology, Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Leskoske</LastName><ForeName>Kristin L</ForeName><Initials>KL</Initials><AffiliationInfo><Affiliation>Division of Biochemistry, Biophysics and Structural Biology, Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Zhang</LastName><ForeName>Lydia H</ForeName><Initials>LH</Initials><AffiliationInfo><Affiliation>Division of Biochemistry, Biophysics and Structural Biology, Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Li</LastName><ForeName>Biyun</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Division of Biochemistry, Biophysics and Structural Biology, Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Thorner</LastName><ForeName>Jeremy</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Division of Biochemistry, Biophysics and Structural Biology, Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01 GM021841</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>S10 OD018136</GrantID><Acronym>OD</Acronym><Agency>NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>T32 GM007232</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., Extramural</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2019</Year><Month>04</Month><Day>10</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Mol Biol Cell</MedlineTA><NlmUniqueID>9201390</NlmUniqueID><ISSNLinking>1059-1524</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D051186">Armadillo Domain Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C503706">Avo1 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D002352">Carrier Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D019269">Phosphatidylinositol 4,5-Diphosphate</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D021122">Protein Subunits</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029701">Saccharomyces cerevisiae Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C504817">TSC11 protein, S cerevisiae</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><CommentsCorrectionsList><CommentsCorrections RefType="ErratumIn"><RefSource>Mol Biol Cell. 2019 Dec 1;30(25):3074</RefSource><PMID Version="1">31778346</PMID></CommentsCorrections></CommentsCorrectionsList><MeshHeadingList><MeshHeading><DescriptorName UI="D051186" MajorTopicYN="N">Armadillo Domain Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002352" MajorTopicYN="N">Carrier Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002462" MajorTopicYN="N">Cell Membrane</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000076225" MajorTopicYN="N">Mechanistic Target of Rapamycin Complex 2</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019269" MajorTopicYN="N">Phosphatidylinositol 4,5-Diphosphate</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000072417" MajorTopicYN="N">Protein 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Leskoske</name><name sortKey="Li, Biyun" sort="Li, Biyun" uniqKey="Li B" first="Biyun" last="Li">Biyun Li</name><name sortKey="Thorner, Jeremy" sort="Thorner, Jeremy" uniqKey="Thorner J" first="Jeremy" last="Thorner">Jeremy Thorner</name><name sortKey="Zhang, Lydia H" sort="Zhang, Lydia H" uniqKey="Zhang L" first="Lydia H" last="Zhang">Lydia H. Zhang</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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