RapamycinFungusV1, Main, Exploration, bibRecord, 000715

The TORC2-Dependent Signaling Network in the Yeast Saccharomyces cerevisiae.

Identifieur interne : 000715 ( Main/Exploration ); précédent : 000714; suivant : 000716

The TORC2-Dependent Signaling Network in the Yeast Saccharomyces cerevisiae.

Auteurs : Françoise M. Roelants [États-Unis] ; Kristin L. Leskoske [États-Unis] ; Maria Nieves Martinez Marshall [États-Unis] ; Melissa N. Locke [États-Unis] ; Jeremy Thorner [États-Unis]

Source :

Biomolecules [ 2218-273X ] ; 2017.

RBID : pubmed:28872598

Descripteurs français

English descriptors

Abstract

To grow, eukaryotic cells must expand by inserting glycerolipids, sphingolipids, sterols, and proteins into their plasma membrane, and maintain the proper levels and bilayer distribution. A fungal cell must coordinate growth with enlargement of its cell wall. In Saccharomyces cerevisiae, a plasma membrane-localized protein kinase complex, Target of Rapamicin (TOR) complex-2 (TORC2) (mammalian ortholog is mTORC2), serves as a sensor and masterregulator of these plasma membrane- and cell wall-associated events by directly phosphorylating and thereby stimulating the activity of two types of effector protein kinases: Ypk1 (mammalian ortholog is SGK1), along with a paralog (Ypk2); and, Pkc1 (mammalian ortholog is PKN2/PRK2). Ypk1 is a central regulator of pathways and processes required for plasma membrane lipid and protein homeostasis, and requires phosphorylation on its T-loop by eisosome-associated protein kinase Pkh1 (mammalian ortholog is PDK1) and a paralog (Pkh2). For cell survival under various stresses, Ypk1 function requires TORC2-mediated phosphorylation at multiple sites near its C terminus. Pkc1 controls diverse processes, especially cell wall synthesis and integrity. Pkc1 is also regulated by Pkh1- and TORC2-dependent phosphorylation, but, in addition, by interaction with Rho1-GTP and lipids phosphatidylserine (PtdSer) and diacylglycerol (DAG). We also describe here what is currently known about the downstream substrates modulated by Ypk1-mediated and Pkc1-mediated phosphorylation.

DOI: 10.3390/biom7030066
PubMed: 28872598
PubMed Central: PMC5618247

Affiliations:

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Le document en format XML

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<term>Cell Wall (metabolism)</term>
<term>Gene Expression Regulation, Fungal (MeSH)</term>
<term>Gene Regulatory Networks (MeSH)</term>
<term>Glycogen Synthase Kinase 3 (chemistry)</term>
<term>Glycogen Synthase Kinase 3 (metabolism)</term>
<term>Mechanistic Target of Rapamycin Complex 2 (chemistry)</term>
<term>Mechanistic Target of Rapamycin Complex 2 (metabolism)</term>
<term>Phosphorylation (MeSH)</term>
<term>Protein Binding (MeSH)</term>
<term>Protein Kinase C (metabolism)</term>
<term>Protein Kinases (metabolism)</term>
<term>Saccharomyces cerevisiae (cytology)</term>
<term>Saccharomyces cerevisiae (growth & development)</term>
<term>Saccharomyces cerevisiae (metabolism)</term>
<term>Saccharomyces cerevisiae Proteins (chemistry)</term>
<term>Saccharomyces cerevisiae Proteins (metabolism)</term>
<term>Signal Transduction (MeSH)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Complexe-2 cible mécanistique de la rapamycine (composition chimique)</term>
<term>Complexe-2 cible mécanistique de la rapamycine (métabolisme)</term>
<term>Glycogen Synthase Kinase 3 (composition chimique)</term>
<term>Glycogen Synthase Kinase 3 (métabolisme)</term>
<term>Liaison aux protéines (MeSH)</term>
<term>Membrane cellulaire (métabolisme)</term>
<term>Paroi cellulaire (métabolisme)</term>
<term>Phosphorylation (MeSH)</term>
<term>Protein kinases (métabolisme)</term>
<term>Protéine kinase C (métabolisme)</term>
<term>Protéines de Saccharomyces cerevisiae (composition chimique)</term>
<term>Protéines de Saccharomyces cerevisiae (métabolisme)</term>
<term>Régulation de l'expression des gènes fongiques (MeSH)</term>
<term>Réseaux de régulation génique (MeSH)</term>
<term>Saccharomyces cerevisiae (croissance et développement)</term>
<term>Saccharomyces cerevisiae (cytologie)</term>
<term>Saccharomyces cerevisiae (métabolisme)</term>
<term>Transduction du signal (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Glycogen Synthase Kinase 3</term>
<term>Mechanistic Target of Rapamycin Complex 2</term>
<term>Saccharomyces cerevisiae Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Complexe-2 cible mécanistique de la rapamycine</term>
<term>Glycogen Synthase Kinase 3</term>
<term>Protéines de Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="croissance et développement" xml:lang="fr"><term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="cytologie" xml:lang="fr"><term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="cytology" xml:lang="en"><term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="growth & development" xml:lang="en"><term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cell Membrane</term>
<term>Cell Wall</term>
<term>Glycogen Synthase Kinase 3</term>
<term>Mechanistic Target of Rapamycin Complex 2</term>
<term>Protein Kinase C</term>
<term>Protein Kinases</term>
<term>Saccharomyces cerevisiae</term>
<term>Saccharomyces cerevisiae Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Complexe-2 cible mécanistique de la rapamycine</term>
<term>Glycogen Synthase Kinase 3</term>
<term>Membrane cellulaire</term>
<term>Paroi cellulaire</term>
<term>Protein kinases</term>
<term>Protéine kinase C</term>
<term>Protéines de Saccharomyces cerevisiae</term>
<term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Gene Expression Regulation, Fungal</term>
<term>Gene Regulatory Networks</term>
<term>Phosphorylation</term>
<term>Protein Binding</term>
<term>Signal Transduction</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Liaison aux protéines</term>
<term>Phosphorylation</term>
<term>Régulation de l'expression des gènes fongiques</term>
<term>Réseaux de régulation génique</term>
<term>Transduction du signal</term>
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<front><div type="abstract" xml:lang="en">To grow, eukaryotic cells must expand by inserting glycerolipids, sphingolipids, sterols, and proteins into their plasma membrane, and maintain the proper levels and bilayer distribution. A fungal cell must coordinate growth with enlargement of its cell wall. In Saccharomyces cerevisiae, a plasma membrane-localized protein kinase complex, Target of Rapamicin (TOR) complex-2 (TORC2) (mammalian ortholog is mTORC2), serves as a sensor and masterregulator of these plasma membrane- and cell wall-associated events by directly phosphorylating and thereby stimulating the activity of two types of effector protein kinases: Ypk1 (mammalian ortholog is SGK1), along with a paralog (Ypk2); and, Pkc1 (mammalian ortholog is PKN2/PRK2). Ypk1 is a central regulator of pathways and processes required for plasma membrane lipid and protein homeostasis, and requires phosphorylation on its T-loop by eisosome-associated protein kinase Pkh1 (mammalian ortholog is PDK1) and a paralog (Pkh2). For cell survival under various stresses, Ypk1 function requires TORC2-mediated phosphorylation at multiple sites near its C terminus. Pkc1 controls diverse processes, especially cell wall synthesis and integrity. Pkc1 is also regulated by Pkh1- and TORC2-dependent phosphorylation, but, in addition, by interaction with Rho1-GTP and lipids phosphatidylserine (PtdSer) and diacylglycerol (DAG). We also describe here what is currently known about the downstream substrates modulated by Ypk1-mediated and Pkc1-mediated phosphorylation.</div>
</front>
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<DateCompleted><Year>2018</Year>
<Month>02</Month>
<Day>28</Day>
</DateCompleted>
<DateRevised><Year>2019</Year>
<Month>01</Month>
<Day>16</Day>
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<JournalIssue CitedMedium="Internet"><Volume>7</Volume>
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<Month>09</Month>
<Day>05</Day>
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<Title>Biomolecules</Title>
<ISOAbbreviation>Biomolecules</ISOAbbreviation>
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<ArticleTitle>The TORC2-Dependent Signaling Network in the Yeast Saccharomyces cerevisiae.</ArticleTitle>
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<Abstract><AbstractText>To grow, eukaryotic cells must expand by inserting glycerolipids, sphingolipids, sterols, and proteins into their plasma membrane, and maintain the proper levels and bilayer distribution. A fungal cell must coordinate growth with enlargement of its cell wall. In Saccharomyces cerevisiae, a plasma membrane-localized protein kinase complex, Target of Rapamicin (TOR) complex-2 (TORC2) (mammalian ortholog is mTORC2), serves as a sensor and masterregulator of these plasma membrane- and cell wall-associated events by directly phosphorylating and thereby stimulating the activity of two types of effector protein kinases: Ypk1 (mammalian ortholog is SGK1), along with a paralog (Ypk2); and, Pkc1 (mammalian ortholog is PKN2/PRK2). Ypk1 is a central regulator of pathways and processes required for plasma membrane lipid and protein homeostasis, and requires phosphorylation on its T-loop by eisosome-associated protein kinase Pkh1 (mammalian ortholog is PDK1) and a paralog (Pkh2). For cell survival under various stresses, Ypk1 function requires TORC2-mediated phosphorylation at multiple sites near its C terminus. Pkc1 controls diverse processes, especially cell wall synthesis and integrity. Pkc1 is also regulated by Pkh1- and TORC2-dependent phosphorylation, but, in addition, by interaction with Rho1-GTP and lipids phosphatidylserine (PtdSer) and diacylglycerol (DAG). We also describe here what is currently known about the downstream substrates modulated by Ypk1-mediated and Pkc1-mediated phosphorylation.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Roelants</LastName>
<ForeName>Françoise M</ForeName>
<Initials>FM</Initials>
<AffiliationInfo><Affiliation>Division of Biochemistry, Biophysics and Structural Biology and Division of Cell and Developmental Biology, Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720-3202, USA. roelants@berkeley.edu.</Affiliation>
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<ForeName>Kristin L</ForeName>
<Initials>KL</Initials>
<AffiliationInfo><Affiliation>Division of Biochemistry, Biophysics and Structural Biology and Division of Cell and Developmental Biology, Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720-3202, USA. kleskoske@berkeley.edu.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Martinez Marshall</LastName>
<ForeName>Maria Nieves</ForeName>
<Initials>MN</Initials>
<AffiliationInfo><Affiliation>Division of Biochemistry, Biophysics and Structural Biology and Division of Cell and Developmental Biology, Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720-3202, USA. nmartinezm@berkeley.edu.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Locke</LastName>
<ForeName>Melissa N</ForeName>
<Initials>MN</Initials>
<AffiliationInfo><Affiliation>Division of Biochemistry, Biophysics and Structural Biology and Division of Cell and Developmental Biology, Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720-3202, USA. mnlocke@berkeley.edu.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Thorner</LastName>
<ForeName>Jeremy</ForeName>
<Initials>J</Initials>
<AffiliationInfo><Affiliation>Division of Biochemistry, Biophysics and Structural Biology and Division of Cell and Developmental Biology, Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720-3202, USA. jthorner@berkeley.edu.</Affiliation>
</AffiliationInfo>
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<GrantList CompleteYN="Y"><Grant><GrantID>R01 GM021841</GrantID>
<Acronym>GM</Acronym>
<Agency>NIGMS NIH HHS</Agency>
<Country>United States</Country>
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<Grant><GrantID>T32 GM007232</GrantID>
<Acronym>GM</Acronym>
<Agency>NIGMS NIH HHS</Agency>
<Country>United States</Country>
</Grant>
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<ArticleDate DateType="Electronic"><Year>2017</Year>
<Month>09</Month>
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<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D029701">Saccharomyces cerevisiae Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 2.7.-</RegistryNumber>
<NameOfSubstance UI="D011494">Protein Kinases</NameOfSubstance>
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<Chemical><RegistryNumber>EC 2.7.1.-</RegistryNumber>
<NameOfSubstance UI="C060388">YPK2 protein, S cerevisiae</NameOfSubstance>
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<NameOfSubstance UI="D000076225">Mechanistic Target of Rapamycin Complex 2</NameOfSubstance>
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<Chemical><RegistryNumber>EC 2.7.12.1</RegistryNumber>
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<MeshHeadingList><MeshHeading><DescriptorName UI="D002462" MajorTopicYN="N">Cell Membrane</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002473" MajorTopicYN="N">Cell Wall</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D015966" MajorTopicYN="N">Gene Expression Regulation, Fungal</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D053263" MajorTopicYN="Y">Gene Regulatory Networks</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D038362" MajorTopicYN="N">Glycogen Synthase Kinase 3</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
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<MeshHeading><DescriptorName UI="D000076225" MajorTopicYN="N">Mechanistic Target of Rapamycin Complex 2</DescriptorName>
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<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
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<MeshHeading><DescriptorName UI="D010766" MajorTopicYN="N">Phosphorylation</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName>
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<MeshHeading><DescriptorName UI="D011493" MajorTopicYN="N">Protein Kinase C</DescriptorName>
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The TORC2-Dependent Signaling Network in the Yeast Saccharomyces cerevisiae.

The TORC2-Dependent Signaling Network in the Yeast Saccharomyces cerevisiae.

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