RapamycinFungusV1, Main, Exploration, bibRecord, 000468

Target of rapamycin complex 2-dependent phosphorylation of the coat protein Pan1 by Akl1 controls endocytosis dynamics in Saccharomyces cerevisiae.

Identifieur interne : 000468 ( Main/Exploration ); précédent : 000467; suivant : 000469

Target of rapamycin complex 2-dependent phosphorylation of the coat protein Pan1 by Akl1 controls endocytosis dynamics in Saccharomyces cerevisiae.

Auteurs : Clélia Bourgoint [Suisse] ; Delphine Rispal [Suisse] ; Marina Berti [Suisse] ; Ireos Filipuzzi [Suisse] ; Stephen B. Helliwell [Suisse] ; Manoël Prouteau [Suisse] ; Robbie Loewith [Suisse]

Source :

The Journal of biological chemistry [ 1083-351X ] ; 2018.

RBID : pubmed:29895620

Descripteurs français

English descriptors

KwdEn :
- Actin Cytoskeleton (drug effects), Actin Cytoskeleton (metabolism), Actin Cytoskeleton (ultrastructure), Cell Membrane (drug effects), Cell Membrane (metabolism), Cell Membrane (ultrastructure), Endocytosis (drug effects), Endocytosis (genetics), Gene Expression Regulation, Fungal (MeSH), Glycerol (metabolism), Glycogen Synthase Kinase 3 (genetics), Glycogen Synthase Kinase 3 (metabolism), Mechanistic Target of Rapamycin Complex 2 (antagonists & inhibitors), Mechanistic Target of Rapamycin Complex 2 (genetics), Mechanistic Target of Rapamycin Complex 2 (metabolism), Microfilament Proteins (genetics), Microfilament Proteins (metabolism), Phosphorylation (drug effects), Protein Kinase Inhibitors (pharmacology), Protein Kinases (genetics), Protein Kinases (metabolism), Saccharomyces cerevisiae (drug effects), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae (ultrastructure), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism), Serine (metabolism), Signal Transduction (MeSH), Sphingolipids (biosynthesis).
MESH :
- chemical , antagonists & inhibitors : Mechanistic Target of Rapamycin Complex 2.
- chemical , biosynthesis : Sphingolipids.
- chemical , genetics : Glycogen Synthase Kinase 3, Mechanistic Target of Rapamycin Complex 2, Microfilament Proteins, Protein Kinases, Saccharomyces cerevisiae Proteins.
- chemical , metabolism : Glycerol, Glycogen Synthase Kinase 3, Mechanistic Target of Rapamycin Complex 2, Microfilament Proteins, Protein Kinases, Saccharomyces cerevisiae Proteins, Serine.
- drug effects : Actin Cytoskeleton, Cell Membrane, Endocytosis, Phosphorylation, Saccharomyces cerevisiae.
- genetics : Endocytosis, Saccharomyces cerevisiae.
- metabolism : Actin Cytoskeleton, Cell Membrane, Saccharomyces cerevisiae.
- chemical , pharmacology : Protein Kinase Inhibitors.
- ultrastructure : Actin Cytoskeleton, Cell Membrane, Saccharomyces cerevisiae.
- Gene Expression Regulation, Fungal, Signal Transduction.

Abstract

Target of rapamycin complex 2 (TORC2) is a widely conserved serine/threonine protein kinase. In the yeast Saccharomyces cerevisiae, TORC2 is essential, playing a key role in plasma membrane homeostasis. In this role, TORC2 regulates diverse processes, including sphingolipid synthesis, glycerol production and efflux, polarization of the actin cytoskeleton, and endocytosis. The major direct substrate of TORC2 is the AGC-family kinase Ypk1. Ypk1 connects TORC2 signaling to actin polarization and to endocytosis via the flippase kinases Fpk1 and Fpk2. Here, we report that Fpk1 mediates TORC2 signaling to control actin polarization, but not endocytosis, via aminophospholipid flippases. To search for specific targets of these flippase kinases, we exploited the fact that Fpk1 prefers to phosphorylate Ser residues within the sequence RXS(L/Y)(D/E), which is present ∼90 times in the yeast proteome. We observed that 25 of these sequences are phosphorylated by Fpk1 in vitro We focused on one sequence hit, the Ark/Prk-family kinase Akl1, as this kinase previously has been implicated in endocytosis. Using a potent ATP-competitive small molecule, CMB4563, to preferentially inhibit TORC2, we found that Fpk1-mediated Akl1 phosphorylation inhibits Akl1 activity, which, in turn, reduces phosphorylation of Pan1 and of other endocytic coat proteins and ultimately contributes to a slowing of endocytosis kinetics. These results indicate that the regulation of actin polarization and endocytosis downstream of TORC2 is signaled through separate pathways that bifurcate at the level of the flippase kinases.

DOI: 10.1074/jbc.RA117.001615
PubMed: 29895620
PubMed Central: PMC6078453

Affiliations:

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Le document en format XML

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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Actin Cytoskeleton (drug effects)</term>
<term>Actin Cytoskeleton (metabolism)</term>
<term>Actin Cytoskeleton (ultrastructure)</term>
<term>Cell Membrane (drug effects)</term>
<term>Cell Membrane (metabolism)</term>
<term>Cell Membrane (ultrastructure)</term>
<term>Endocytosis (drug effects)</term>
<term>Endocytosis (genetics)</term>
<term>Gene Expression Regulation, Fungal (MeSH)</term>
<term>Glycerol (metabolism)</term>
<term>Glycogen Synthase Kinase 3 (genetics)</term>
<term>Glycogen Synthase Kinase 3 (metabolism)</term>
<term>Mechanistic Target of Rapamycin Complex 2 (antagonists & inhibitors)</term>
<term>Mechanistic Target of Rapamycin Complex 2 (genetics)</term>
<term>Mechanistic Target of Rapamycin Complex 2 (metabolism)</term>
<term>Microfilament Proteins (genetics)</term>
<term>Microfilament Proteins (metabolism)</term>
<term>Phosphorylation (drug effects)</term>
<term>Protein Kinase Inhibitors (pharmacology)</term>
<term>Protein Kinases (genetics)</term>
<term>Protein Kinases (metabolism)</term>
<term>Saccharomyces cerevisiae (drug effects)</term>
<term>Saccharomyces cerevisiae (genetics)</term>
<term>Saccharomyces cerevisiae (metabolism)</term>
<term>Saccharomyces cerevisiae (ultrastructure)</term>
<term>Saccharomyces cerevisiae Proteins (genetics)</term>
<term>Saccharomyces cerevisiae Proteins (metabolism)</term>
<term>Serine (metabolism)</term>
<term>Signal Transduction (MeSH)</term>
<term>Sphingolipids (biosynthesis)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Complexe-2 cible mécanistique de la rapamycine (antagonistes et inhibiteurs)</term>
<term>Complexe-2 cible mécanistique de la rapamycine (génétique)</term>
<term>Complexe-2 cible mécanistique de la rapamycine (métabolisme)</term>
<term>Cytosquelette d'actine (effets des médicaments et des substances chimiques)</term>
<term>Cytosquelette d'actine (métabolisme)</term>
<term>Cytosquelette d'actine (ultrastructure)</term>
<term>Endocytose (effets des médicaments et des substances chimiques)</term>
<term>Endocytose (génétique)</term>
<term>Glycogen Synthase Kinase 3 (génétique)</term>
<term>Glycogen Synthase Kinase 3 (métabolisme)</term>
<term>Glycérol (métabolisme)</term>
<term>Inhibiteurs de protéines kinases (pharmacologie)</term>
<term>Membrane cellulaire (effets des médicaments et des substances chimiques)</term>
<term>Membrane cellulaire (métabolisme)</term>
<term>Membrane cellulaire (ultrastructure)</term>
<term>Phosphorylation (effets des médicaments et des substances chimiques)</term>
<term>Protein kinases (génétique)</term>
<term>Protein kinases (métabolisme)</term>
<term>Protéines de Saccharomyces cerevisiae (génétique)</term>
<term>Protéines de Saccharomyces cerevisiae (métabolisme)</term>
<term>Protéines des microfilaments (génétique)</term>
<term>Protéines des microfilaments (métabolisme)</term>
<term>Régulation de l'expression des gènes fongiques (MeSH)</term>
<term>Saccharomyces cerevisiae (effets des médicaments et des substances chimiques)</term>
<term>Saccharomyces cerevisiae (génétique)</term>
<term>Saccharomyces cerevisiae (métabolisme)</term>
<term>Saccharomyces cerevisiae (ultrastructure)</term>
<term>Sphingolipides (biosynthèse)</term>
<term>Sérine (métabolisme)</term>
<term>Transduction du signal (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Mechanistic Target of Rapamycin Complex 2</term>
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<keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Sphingolipids</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Glycogen Synthase Kinase 3</term>
<term>Mechanistic Target of Rapamycin Complex 2</term>
<term>Microfilament Proteins</term>
<term>Protein Kinases</term>
<term>Saccharomyces cerevisiae Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glycerol</term>
<term>Glycogen Synthase Kinase 3</term>
<term>Mechanistic Target of Rapamycin Complex 2</term>
<term>Microfilament Proteins</term>
<term>Protein Kinases</term>
<term>Saccharomyces cerevisiae Proteins</term>
<term>Serine</term>
</keywords>
<keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Complexe-2 cible mécanistique de la rapamycine</term>
</keywords>
<keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Sphingolipides</term>
</keywords>
<keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Actin Cytoskeleton</term>
<term>Cell Membrane</term>
<term>Endocytosis</term>
<term>Phosphorylation</term>
<term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Cytosquelette d'actine</term>
<term>Endocytose</term>
<term>Membrane cellulaire</term>
<term>Phosphorylation</term>
<term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Endocytosis</term>
<term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Complexe-2 cible mécanistique de la rapamycine</term>
<term>Endocytose</term>
<term>Glycogen Synthase Kinase 3</term>
<term>Protein kinases</term>
<term>Protéines de Saccharomyces cerevisiae</term>
<term>Protéines des microfilaments</term>
<term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Actin Cytoskeleton</term>
<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>Cytosquelette d'actine</term>
<term>Glycogen Synthase Kinase 3</term>
<term>Glycérol</term>
<term>Membrane cellulaire</term>
<term>Protein kinases</term>
<term>Protéines de Saccharomyces cerevisiae</term>
<term>Protéines des microfilaments</term>
<term>Saccharomyces cerevisiae</term>
<term>Sérine</term>
</keywords>
<keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Inhibiteurs de protéines kinases</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Protein Kinase Inhibitors</term>
</keywords>
<keywords scheme="MESH" qualifier="ultrastructure" xml:lang="en"><term>Actin Cytoskeleton</term>
<term>Cell Membrane</term>
<term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Gene Expression Regulation, Fungal</term>
<term>Signal Transduction</term>
</keywords>
<keywords scheme="MESH" qualifier="ultrastructure" xml:lang="fr"><term>Cytosquelette d'actine</term>
<term>Membrane cellulaire</term>
<term>Régulation de l'expression des gènes fongiques</term>
<term>Saccharomyces cerevisiae</term>
<term>Transduction du signal</term>
</keywords>
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<front><div type="abstract" xml:lang="en">Target of rapamycin complex 2 (TORC2) is a widely conserved serine/threonine protein kinase. In the yeast <i>Saccharomyces cerevisiae</i>
, TORC2 is essential, playing a key role in plasma membrane homeostasis. In this role, TORC2 regulates diverse processes, including sphingolipid synthesis, glycerol production and efflux, polarization of the actin cytoskeleton, and endocytosis. The major direct substrate of TORC2 is the AGC-family kinase Ypk1. Ypk1 connects TORC2 signaling to actin polarization and to endocytosis via the flippase kinases Fpk1 and Fpk2. Here, we report that Fpk1 mediates TORC2 signaling to control actin polarization, but not endocytosis, via aminophospholipid flippases. To search for specific targets of these flippase kinases, we exploited the fact that Fpk1 prefers to phosphorylate Ser residues within the sequence R<i>X</i>
S(L/Y)(D/E), which is present ∼90 times in the yeast proteome. We observed that 25 of these sequences are phosphorylated by Fpk1 <i>in vitro</i>
 We focused on one sequence hit, the Ark/Prk-family kinase Akl1, as this kinase previously has been implicated in endocytosis. Using a potent ATP-competitive small molecule, CMB4563, to preferentially inhibit TORC2, we found that Fpk1-mediated Akl1 phosphorylation inhibits Akl1 activity, which, in turn, reduces phosphorylation of Pan1 and of other endocytic coat proteins and ultimately contributes to a slowing of endocytosis kinetics. These results indicate that the regulation of actin polarization and endocytosis downstream of TORC2 is signaled through separate pathways that bifurcate at the level of the flippase kinases.</div>
</front>
</TEI>
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<DateCompleted><Year>2019</Year>
<Month>02</Month>
<Day>08</Day>
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<Month>02</Month>
<Day>15</Day>
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<Issue>31</Issue>
<PubDate><Year>2018</Year>
<Month>08</Month>
<Day>03</Day>
</PubDate>
</JournalIssue>
<Title>The Journal of biological chemistry</Title>
<ISOAbbreviation>J Biol Chem</ISOAbbreviation>
</Journal>
<ArticleTitle>Target of rapamycin complex 2-dependent phosphorylation of the coat protein Pan1 by Akl1 controls endocytosis dynamics in <i>Saccharomyces cerevisiae</i>
.</ArticleTitle>
<Pagination><MedlinePgn>12043-12053</MedlinePgn>
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<ELocationID EIdType="doi" ValidYN="Y">10.1074/jbc.RA117.001615</ELocationID>
<Abstract><AbstractText>Target of rapamycin complex 2 (TORC2) is a widely conserved serine/threonine protein kinase. In the yeast <i>Saccharomyces cerevisiae</i>
, TORC2 is essential, playing a key role in plasma membrane homeostasis. In this role, TORC2 regulates diverse processes, including sphingolipid synthesis, glycerol production and efflux, polarization of the actin cytoskeleton, and endocytosis. The major direct substrate of TORC2 is the AGC-family kinase Ypk1. Ypk1 connects TORC2 signaling to actin polarization and to endocytosis via the flippase kinases Fpk1 and Fpk2. Here, we report that Fpk1 mediates TORC2 signaling to control actin polarization, but not endocytosis, via aminophospholipid flippases. To search for specific targets of these flippase kinases, we exploited the fact that Fpk1 prefers to phosphorylate Ser residues within the sequence R<i>X</i>
S(L/Y)(D/E), which is present ∼90 times in the yeast proteome. We observed that 25 of these sequences are phosphorylated by Fpk1 <i>in vitro</i>
 We focused on one sequence hit, the Ark/Prk-family kinase Akl1, as this kinase previously has been implicated in endocytosis. Using a potent ATP-competitive small molecule, CMB4563, to preferentially inhibit TORC2, we found that Fpk1-mediated Akl1 phosphorylation inhibits Akl1 activity, which, in turn, reduces phosphorylation of Pan1 and of other endocytic coat proteins and ultimately contributes to a slowing of endocytosis kinetics. These results indicate that the regulation of actin polarization and endocytosis downstream of TORC2 is signaled through separate pathways that bifurcate at the level of the flippase kinases.</AbstractText>
<CopyrightInformation>© 2018 by The American Society for Biochemistry and Molecular Biology, Inc.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Bourgoint</LastName>
<ForeName>Clélia</ForeName>
<Initials>C</Initials>
<AffiliationInfo><Affiliation>From the Department of Molecular Biology and Institute of Genetics and Genomics of Geneva (iGE3), National Center for Competence in Research in Chemical Biology, University of Geneva, 1211 Geneva, Switzerland and.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Rispal</LastName>
<ForeName>Delphine</ForeName>
<Initials>D</Initials>
<AffiliationInfo><Affiliation>From the Department of Molecular Biology and Institute of Genetics and Genomics of Geneva (iGE3), National Center for Competence in Research in Chemical Biology, University of Geneva, 1211 Geneva, Switzerland and.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Berti</LastName>
<ForeName>Marina</ForeName>
<Initials>M</Initials>
<AffiliationInfo><Affiliation>From the Department of Molecular Biology and Institute of Genetics and Genomics of Geneva (iGE3), National Center for Competence in Research in Chemical Biology, University of Geneva, 1211 Geneva, Switzerland and.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Filipuzzi</LastName>
<ForeName>Ireos</ForeName>
<Initials>I</Initials>
<AffiliationInfo><Affiliation>Novartis Institutes for Biomedical Research, Novartis Campus, 4056 Basel, Switzerland.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Helliwell</LastName>
<ForeName>Stephen B</ForeName>
<Initials>SB</Initials>
<Identifier Source="ORCID">0000-0001-6019-9574</Identifier>
<AffiliationInfo><Affiliation>Novartis Institutes for Biomedical Research, Novartis Campus, 4056 Basel, Switzerland.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Prouteau</LastName>
<ForeName>Manoël</ForeName>
<Initials>M</Initials>
<AffiliationInfo><Affiliation>From the Department of Molecular Biology and Institute of Genetics and Genomics of Geneva (iGE3), National Center for Competence in Research in Chemical Biology, University of Geneva, 1211 Geneva, Switzerland and manoel.prouteau@unige.ch.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Loewith</LastName>
<ForeName>Robbie</ForeName>
<Initials>R</Initials>
<Identifier Source="ORCID">0000-0002-2482-603X</Identifier>
<AffiliationInfo><Affiliation>From the Department of Molecular Biology and Institute of Genetics and Genomics of Geneva (iGE3), National Center for Competence in Research in Chemical Biology, University of Geneva, 1211 Geneva, Switzerland and robbie.loewith@unige.ch.</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>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2018</Year>
<Month>06</Month>
<Day>12</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>United States</Country>
<MedlineTA>J Biol Chem</MedlineTA>
<NlmUniqueID>2985121R</NlmUniqueID>
<ISSNLinking>0021-9258</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D008840">Microfilament Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="C111870">PAN1 protein, S cerevisiae</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D047428">Protein Kinase Inhibitors</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D029701">Saccharomyces cerevisiae Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D013107">Sphingolipids</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>452VLY9402</RegistryNumber>
<NameOfSubstance UI="D012694">Serine</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 2.7.-</RegistryNumber>
<NameOfSubstance UI="D011494">Protein Kinases</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber>
<NameOfSubstance UI="C533049">Fpk1 protein, S cerevisiae</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber>
<NameOfSubstance UI="C533050">Fpk2 protein, S cerevisiae</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber>
<NameOfSubstance UI="D000076225">Mechanistic Target of Rapamycin Complex 2</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 2.7.11.26</RegistryNumber>
<NameOfSubstance UI="D038362">Glycogen Synthase Kinase 3</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 2.7.12.1</RegistryNumber>
<NameOfSubstance UI="C068124">MCK1 protein, S cerevisiae</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>PDC6A3C0OX</RegistryNumber>
<NameOfSubstance UI="D005990">Glycerol</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D008841" MajorTopicYN="N">Actin Cytoskeleton</DescriptorName>
<QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
<QualifierName UI="Q000648" MajorTopicYN="N">ultrastructure</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002462" MajorTopicYN="N">Cell Membrane</DescriptorName>
<QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
<QualifierName UI="Q000648" MajorTopicYN="N">ultrastructure</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D004705" MajorTopicYN="N">Endocytosis</DescriptorName>
<QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D015966" MajorTopicYN="Y">Gene Expression Regulation, Fungal</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D005990" MajorTopicYN="N">Glycerol</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D038362" MajorTopicYN="N">Glycogen Synthase Kinase 3</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000076225" MajorTopicYN="N">Mechanistic Target of Rapamycin Complex 2</DescriptorName>
<QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008840" MajorTopicYN="N">Microfilament Proteins</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010766" MajorTopicYN="N">Phosphorylation</DescriptorName>
<QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D047428" MajorTopicYN="N">Protein Kinase Inhibitors</DescriptorName>
<QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011494" MajorTopicYN="N">Protein Kinases</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="Q000187" MajorTopicYN="N">drug effects</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
<QualifierName UI="Q000648" MajorTopicYN="N">ultrastructure</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="D012694" MajorTopicYN="N">Serine</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D015398" MajorTopicYN="N">Signal Transduction</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D013107" MajorTopicYN="N">Sphingolipids</DescriptorName>
<QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName>
</MeshHeading>
</MeshHeadingList>
<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">Ark1/Prk1 family</Keyword>
<Keyword MajorTopicYN="Y">Fpk1</Keyword>
<Keyword MajorTopicYN="Y">Pan1</Keyword>
<Keyword MajorTopicYN="Y">actin</Keyword>
<Keyword MajorTopicYN="Y">aminophospholipid flippase</Keyword>
<Keyword MajorTopicYN="Y">endocytosis</Keyword>
<Keyword MajorTopicYN="Y">in vitro kinase assay</Keyword>
<Keyword MajorTopicYN="Y">membrane function</Keyword>
<Keyword MajorTopicYN="Y">signal transduction</Keyword>
<Keyword MajorTopicYN="Y">target of rapamycin (TOR)</Keyword>
</KeywordList>
<CoiStatement>The authors declare that they have no conflicts of interest with the contents of this article.</CoiStatement>
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<affiliations><list><country><li>Suisse</li>
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<tree><country name="Suisse"><region name="Canton de Genève"><name sortKey="Bourgoint, Clelia" sort="Bourgoint, Clelia" uniqKey="Bourgoint C" first="Clélia" last="Bourgoint">Clélia Bourgoint</name>
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<name sortKey="Berti, Marina" sort="Berti, Marina" uniqKey="Berti M" first="Marina" last="Berti">Marina Berti</name>
<name sortKey="Filipuzzi, Ireos" sort="Filipuzzi, Ireos" uniqKey="Filipuzzi I" first="Ireos" last="Filipuzzi">Ireos Filipuzzi</name>
<name sortKey="Helliwell, Stephen B" sort="Helliwell, Stephen B" uniqKey="Helliwell S" first="Stephen B" last="Helliwell">Stephen B. Helliwell</name>
<name sortKey="Loewith, Robbie" sort="Loewith, Robbie" uniqKey="Loewith R" first="Robbie" last="Loewith">Robbie Loewith</name>
<name sortKey="Prouteau, Manoel" sort="Prouteau, Manoel" uniqKey="Prouteau M" first="Manoël" last="Prouteau">Manoël Prouteau</name>
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Target of rapamycin complex 2-dependent phosphorylation of the coat protein Pan1 by Akl1 controls endocytosis dynamics in Saccharomyces cerevisiae.

Target of rapamycin complex 2-dependent phosphorylation of the coat protein Pan1 by Akl1 controls endocytosis dynamics in Saccharomyces cerevisiae.

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