RapamycinFungusV1, Main, Exploration, bibRecord, 000627

Decrease in plasma membrane tension triggers PtdIns(4,5)P2 phase separation to inactivate TORC2.

Identifieur interne : 000627 ( Main/Exploration ); précédent : 000626; suivant : 000628

Decrease in plasma membrane tension triggers PtdIns(4,5)P2 phase separation to inactivate TORC2.

Auteurs : Margot Riggi [Suisse] ; Karolina Niewola-Staszkowska [Suisse] ; Nicolas Chiaruttini [Suisse] ; Adai Colom [Suisse] ; Beata Kusmider [Suisse] ; Vincent Mercier [Suisse] ; Saeideh Soleimanpour [Suisse] ; Michael Stahl [Suisse] ; Stefan Matile [Suisse] ; Aurélien Roux [Suisse] ; Robbie Loewith [Suisse]

Source :

Nature cell biology [ 1476-4679 ] ; 2018.

RBID : pubmed:30154550

Descripteurs français

English descriptors

KwdEn :
- Carrier Proteins (genetics), Carrier Proteins (metabolism), Cell Membrane (drug effects), Cell Membrane (metabolism), Cytoskeletal Proteins (MeSH), Enzyme Activation (MeSH), Fungal Proteins (genetics), Fungal Proteins (metabolism), Kinetics (MeSH), Mechanistic Target of Rapamycin Complex 2 (genetics), Mechanistic Target of Rapamycin Complex 2 (metabolism), Mechanotransduction, Cellular (drug effects), Osmotic Pressure (MeSH), Palmitoylcarnitine (pharmacology), Phosphatidylinositol 4,5-Diphosphate (metabolism), Protein Transport (MeSH), RNA-Binding Proteins (genetics), RNA-Binding Proteins (metabolism), Saccharomyces cerevisiae (drug effects), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism), Second Messenger Systems (drug effects).
MESH :
- chemical , genetics : Carrier Proteins, Fungal Proteins, Mechanistic Target of Rapamycin Complex 2, RNA-Binding Proteins, Saccharomyces cerevisiae Proteins.
- chemical , metabolism : Carrier Proteins, Fungal Proteins, Mechanistic Target of Rapamycin Complex 2, Phosphatidylinositol 4,5-Diphosphate, RNA-Binding Proteins, Saccharomyces cerevisiae Proteins.
- drug effects : Cell Membrane, Mechanotransduction, Cellular, Saccharomyces cerevisiae, Second Messenger Systems.
- genetics : Saccharomyces cerevisiae.
- metabolism : Cell Membrane, Saccharomyces cerevisiae.
- chemical , pharmacology : Palmitoylcarnitine.
- chemical : Cytoskeletal Proteins, Enzyme Activation, Kinetics, Osmotic Pressure, Protein Transport.

Abstract

The target of rapamycin complex 2 (TORC2) plays a key role in maintaining the homeostasis of plasma membrane (PM) tension. TORC2 activation following increased PM tension involves redistribution of the Slm1 and 2 paralogues from PM invaginations known as eisosomes into membrane compartments containing TORC2. How Slm1/2 relocalization is triggered, and if/how this plays a role in TORC2 inactivation with decreased PM tension, is unknown. Using osmotic shocks and palmitoylcarnitine as orthogonal tools to manipulate PM tension, we demonstrate that decreased PM tension triggers spontaneous, energy-independent reorganization of pre-existing phosphatidylinositol-4,5-bisphosphate into discrete invaginated membrane domains, which cluster and inactivate TORC2. These results demonstrate that increased and decreased membrane tension are sensed through different mechanisms, highlighting a role for membrane lipid phase separation in mechanotransduction.

DOI: 10.1038/s41556-018-0150-z
PubMed: 30154550
PubMed Central: PMC6237274

Affiliations:

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Le document en format XML

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 phase separation to inactivate TORC2.</title>
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<author><name sortKey="Loewith, Robbie" sort="Loewith, Robbie" uniqKey="Loewith R" first="Robbie" last="Loewith">Robbie Loewith</name>
<affiliation wicri:level="4"><nlm:affiliation>Department of Molecular Biology, University of Geneva, Geneva, Switzerland. robbie.loewith@unige.ch.</nlm:affiliation>
<country xml:lang="fr">Suisse</country>
<wicri:regionArea>Department of Molecular Biology, University of Geneva, Geneva</wicri:regionArea>
<orgName type="university">Université de Genève</orgName>
<placeName><settlement type="city">Genève</settlement>
<region nuts="3" type="region">Canton de Genève</region>
</placeName>
</affiliation>
<affiliation wicri:level="1"><nlm:affiliation>iGE3 Institute of Genetics and Genomics of Geneva, Geneva, Switzerland. robbie.loewith@unige.ch.</nlm:affiliation>
<country xml:lang="fr">Suisse</country>
<wicri:regionArea>iGE3 Institute of Genetics and Genomics of Geneva, Geneva</wicri:regionArea>
<wicri:noRegion>Geneva</wicri:noRegion>
</affiliation>
<affiliation wicri:level="1"><nlm:affiliation>Swiss National Centre for Competence in Research Program Chemical Biology, Geneva, Switzerland. robbie.loewith@unige.ch.</nlm:affiliation>
<country xml:lang="fr">Suisse</country>
<wicri:regionArea>Swiss National Centre for Competence in Research Program Chemical Biology, Geneva</wicri:regionArea>
<wicri:noRegion>Geneva</wicri:noRegion>
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<series><title level="j">Nature cell biology</title>
<idno type="eISSN">1476-4679</idno>
<imprint><date when="2018" type="published">2018</date>
</imprint>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Carrier Proteins (genetics)</term>
<term>Carrier Proteins (metabolism)</term>
<term>Cell Membrane (drug effects)</term>
<term>Cell Membrane (metabolism)</term>
<term>Cytoskeletal Proteins (MeSH)</term>
<term>Enzyme Activation (MeSH)</term>
<term>Fungal Proteins (genetics)</term>
<term>Fungal Proteins (metabolism)</term>
<term>Kinetics (MeSH)</term>
<term>Mechanistic Target of Rapamycin Complex 2 (genetics)</term>
<term>Mechanistic Target of Rapamycin Complex 2 (metabolism)</term>
<term>Mechanotransduction, Cellular (drug effects)</term>
<term>Osmotic Pressure (MeSH)</term>
<term>Palmitoylcarnitine (pharmacology)</term>
<term>Phosphatidylinositol 4,5-Diphosphate (metabolism)</term>
<term>Protein Transport (MeSH)</term>
<term>RNA-Binding Proteins (genetics)</term>
<term>RNA-Binding Proteins (metabolism)</term>
<term>Saccharomyces cerevisiae (drug effects)</term>
<term>Saccharomyces cerevisiae (genetics)</term>
<term>Saccharomyces cerevisiae (metabolism)</term>
<term>Saccharomyces cerevisiae Proteins (genetics)</term>
<term>Saccharomyces cerevisiae Proteins (metabolism)</term>
<term>Second Messenger Systems (drug effects)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Activation enzymatique (MeSH)</term>
<term>Cinétique (MeSH)</term>
<term>Complexe-2 cible mécanistique de la rapamycine (génétique)</term>
<term>Complexe-2 cible mécanistique de la rapamycine (métabolisme)</term>
<term>Membrane cellulaire (effets des médicaments et des substances chimiques)</term>
<term>Membrane cellulaire (métabolisme)</term>
<term>Mécanotransduction cellulaire (effets des médicaments et des substances chimiques)</term>
<term>Palmitoyl-carnitine (pharmacologie)</term>
<term>Phosphatidylinositol diphosphate-4,5 (métabolisme)</term>
<term>Pression osmotique (MeSH)</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>Protéines fongiques (génétique)</term>
<term>Protéines fongiques (métabolisme)</term>
<term>Saccharomyces cerevisiae (effets des médicaments et des substances chimiques)</term>
<term>Saccharomyces cerevisiae (génétique)</term>
<term>Saccharomyces cerevisiae (métabolisme)</term>
<term>Systèmes de seconds messagers (effets des médicaments et des substances chimiques)</term>
<term>Transport des protéines (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Carrier Proteins</term>
<term>Fungal Proteins</term>
<term>Mechanistic Target of Rapamycin Complex 2</term>
<term>RNA-Binding Proteins</term>
<term>Saccharomyces cerevisiae Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Carrier Proteins</term>
<term>Fungal Proteins</term>
<term>Mechanistic Target of Rapamycin Complex 2</term>
<term>Phosphatidylinositol 4,5-Diphosphate</term>
<term>RNA-Binding Proteins</term>
<term>Saccharomyces cerevisiae Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Cell Membrane</term>
<term>Mechanotransduction, Cellular</term>
<term>Saccharomyces cerevisiae</term>
<term>Second Messenger Systems</term>
</keywords>
<keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Membrane cellulaire</term>
<term>Mécanotransduction cellulaire</term>
<term>Saccharomyces cerevisiae</term>
<term>Systèmes de seconds messagers</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Complexe-2 cible mécanistique de la rapamycine</term>
<term>Protéines de Saccharomyces cerevisiae</term>
<term>Protéines de liaison à l'ARN</term>
<term>Protéines de transport</term>
<term>Protéines fongiques</term>
<term>Saccharomyces cerevisiae</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 liaison à l'ARN</term>
<term>Protéines de transport</term>
<term>Protéines fongiques</term>
<term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Palmitoyl-carnitine</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Palmitoylcarnitine</term>
</keywords>
<keywords scheme="MESH" type="chemical" xml:lang="en"><term>Cytoskeletal Proteins</term>
<term>Enzyme Activation</term>
<term>Kinetics</term>
<term>Osmotic Pressure</term>
<term>Protein Transport</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Activation enzymatique</term>
<term>Cinétique</term>
<term>Pression osmotique</term>
<term>Protéines du cytosquelette</term>
<term>Transport des protéines</term>
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<front><div type="abstract" xml:lang="en">The target of rapamycin complex 2 (TORC2) plays a key role in maintaining the homeostasis of plasma membrane (PM) tension. TORC2 activation following increased PM tension involves redistribution of the Slm1 and 2 paralogues from PM invaginations known as eisosomes into membrane compartments containing TORC2. How Slm1/2 relocalization is triggered, and if/how this plays a role in TORC2 inactivation with decreased PM tension, is unknown. Using osmotic shocks and palmitoylcarnitine as orthogonal tools to manipulate PM tension, we demonstrate that decreased PM tension triggers spontaneous, energy-independent reorganization of pre-existing phosphatidylinositol-4,5-bisphosphate into discrete invaginated membrane domains, which cluster and inactivate TORC2. These results demonstrate that increased and decreased membrane tension are sensed through different mechanisms, highlighting a role for membrane lipid phase separation in mechanotransduction.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">30154550</PMID>
<DateCompleted><Year>2019</Year>
<Month>05</Month>
<Day>07</Day>
</DateCompleted>
<DateRevised><Year>2019</Year>
<Month>12</Month>
<Day>10</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1476-4679</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>20</Volume>
<Issue>9</Issue>
<PubDate><Year>2018</Year>
<Month>09</Month>
</PubDate>
</JournalIssue>
<Title>Nature cell biology</Title>
<ISOAbbreviation>Nat Cell Biol</ISOAbbreviation>
</Journal>
<ArticleTitle>Decrease in plasma membrane tension triggers PtdIns(4,5)P<sub>2</sub>
 phase separation to inactivate TORC2.</ArticleTitle>
<Pagination><MedlinePgn>1043-1051</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1038/s41556-018-0150-z</ELocationID>
<Abstract><AbstractText>The target of rapamycin complex 2 (TORC2) plays a key role in maintaining the homeostasis of plasma membrane (PM) tension. TORC2 activation following increased PM tension involves redistribution of the Slm1 and 2 paralogues from PM invaginations known as eisosomes into membrane compartments containing TORC2. How Slm1/2 relocalization is triggered, and if/how this plays a role in TORC2 inactivation with decreased PM tension, is unknown. Using osmotic shocks and palmitoylcarnitine as orthogonal tools to manipulate PM tension, we demonstrate that decreased PM tension triggers spontaneous, energy-independent reorganization of pre-existing phosphatidylinositol-4,5-bisphosphate into discrete invaginated membrane domains, which cluster and inactivate TORC2. These results demonstrate that increased and decreased membrane tension are sensed through different mechanisms, highlighting a role for membrane lipid phase separation in mechanotransduction.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Riggi</LastName>
<ForeName>Margot</ForeName>
<Initials>M</Initials>
<AffiliationInfo><Affiliation>Department of Molecular Biology, University of Geneva, Geneva, Switzerland.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Department of Biochemistry, University of Geneva, Geneva, Switzerland.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>iGE3 Institute of Genetics and Genomics of Geneva, Geneva, Switzerland.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Swiss National Centre for Competence in Research Program Chemical Biology, Geneva, Switzerland.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Niewola-Staszkowska</LastName>
<ForeName>Karolina</ForeName>
<Initials>K</Initials>
<AffiliationInfo><Affiliation>Department of Molecular Biology, University of Geneva, Geneva, Switzerland.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Swiss National Centre for Competence in Research Program Chemical Biology, Geneva, Switzerland.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Chiaruttini</LastName>
<ForeName>Nicolas</ForeName>
<Initials>N</Initials>
<AffiliationInfo><Affiliation>Department of Biochemistry, University of Geneva, Geneva, Switzerland.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Colom</LastName>
<ForeName>Adai</ForeName>
<Initials>A</Initials>
<AffiliationInfo><Affiliation>Department of Biochemistry, University of Geneva, Geneva, Switzerland.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Swiss National Centre for Competence in Research Program Chemical Biology, Geneva, Switzerland.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Kusmider</LastName>
<ForeName>Beata</ForeName>
<Initials>B</Initials>
<AffiliationInfo><Affiliation>Department of Molecular Biology, University of Geneva, Geneva, Switzerland.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Mercier</LastName>
<ForeName>Vincent</ForeName>
<Initials>V</Initials>
<AffiliationInfo><Affiliation>Department of Biochemistry, University of Geneva, Geneva, Switzerland.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Swiss National Centre for Competence in Research Program Chemical Biology, Geneva, Switzerland.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Soleimanpour</LastName>
<ForeName>Saeideh</ForeName>
<Initials>S</Initials>
<AffiliationInfo><Affiliation>Swiss National Centre for Competence in Research Program Chemical Biology, Geneva, Switzerland.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Department of Organic Chemistry, University of Geneva, Geneva, Switzerland.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Stahl</LastName>
<ForeName>Michael</ForeName>
<Initials>M</Initials>
<AffiliationInfo><Affiliation>Department of Molecular Biology, University of Geneva, Geneva, Switzerland.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Matile</LastName>
<ForeName>Stefan</ForeName>
<Initials>S</Initials>
<AffiliationInfo><Affiliation>Swiss National Centre for Competence in Research Program Chemical Biology, Geneva, Switzerland.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Department of Organic Chemistry, University of Geneva, Geneva, Switzerland.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Roux</LastName>
<ForeName>Aurélien</ForeName>
<Initials>A</Initials>
<Identifier Source="ORCID">http://orcid.org/0000-0002-6088-0711</Identifier>
<AffiliationInfo><Affiliation>Department of Biochemistry, University of Geneva, Geneva, Switzerland. aurelien.roux@unige.ch.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Swiss National Centre for Competence in Research Program Chemical Biology, Geneva, Switzerland. aurelien.roux@unige.ch.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Loewith</LastName>
<ForeName>Robbie</ForeName>
<Initials>R</Initials>
<Identifier Source="ORCID">http://orcid.org/0000-0002-2482-603X</Identifier>
<AffiliationInfo><Affiliation>Department of Molecular Biology, University of Geneva, Geneva, Switzerland. robbie.loewith@unige.ch.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>iGE3 Institute of Genetics and Genomics of Geneva, Geneva, Switzerland. robbie.loewith@unige.ch.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Swiss National Centre for Competence in Research Program Chemical Biology, Geneva, Switzerland. robbie.loewith@unige.ch.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
<GrantList CompleteYN="Y"><Grant><GrantID>311536</GrantID>
<Agency>European Research Council</Agency>
<Country>International</Country>
</Grant>
<Grant><GrantID>160023</GrantID>
<Agency>Swiss National Science Foundation</Agency>
<Country>Switzerland</Country>
</Grant>
<Grant><GrantID>149975</GrantID>
<Agency>Swiss National Science Foundation</Agency>
<Country>Switzerland</Country>
</Grant>
<Grant><GrantID>130520</GrantID>
<Agency>Swiss National Science Foundation</Agency>
<Country>Switzerland</Country>
</Grant>
<Grant><GrantID>173087</GrantID>
<Agency>Swiss National Science Foundation</Agency>
<Country>Switzerland</Country>
</Grant>
<Grant><GrantID>614552</GrantID>
<Agency>European Research Council</Agency>
<Country>International</Country>
</Grant>
</GrantList>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2018</Year>
<Month>08</Month>
<Day>27</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>England</Country>
<MedlineTA>Nat Cell Biol</MedlineTA>
<NlmUniqueID>100890575</NlmUniqueID>
<ISSNLinking>1465-7392</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><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="D005656">Fungal Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
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<Chemical><RegistryNumber>0</RegistryNumber>
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<Chemical><RegistryNumber>1935-18-8</RegistryNumber>
<NameOfSubstance UI="D010172">Palmitoylcarnitine</NameOfSubstance>
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<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
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<MeshHeading><DescriptorName UI="D002462" MajorTopicYN="N">Cell Membrane</DescriptorName>
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<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D003598" MajorTopicYN="N">Cytoskeletal Proteins</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D004789" MajorTopicYN="N">Enzyme Activation</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName>
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<QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D019269" MajorTopicYN="N">Phosphatidylinositol 4,5-Diphosphate</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D021381" MajorTopicYN="N">Protein Transport</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D016601" MajorTopicYN="N">RNA-Binding Proteins</DescriptorName>
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</MeshHeading>
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</MeshHeading>
<MeshHeading><DescriptorName UI="D015290" MajorTopicYN="Y">Second Messenger Systems</DescriptorName>
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	Serveur d'exploration sur la rapamycine et les champignons
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Decrease in plasma membrane tension triggers PtdIns(4,5)P2 phase separation to inactivate TORC2.

Decrease in plasma membrane tension triggers PtdIns(4,5)P2 phase separation to inactivate TORC2.

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