TORC1 controls G1-S cell cycle transition in yeast via Mpk1 and the greatwall kinase pathway.
Identifieur interne : 000C09 ( Main/Exploration ); précédent : 000C08; suivant : 000C10TORC1 controls G1-S cell cycle transition in yeast via Mpk1 and the greatwall kinase pathway.
Auteurs : Marta Moreno-Torres [Suisse] ; Malika Jaquenoud [Suisse] ; Claudio De Virgilio [Suisse]Source :
- Nature communications [ 2041-1723 ] ; 2015.
Descripteurs français
- KwdFr :
- Complexe-1 cible mécanistique de la rapamycine (MeSH), Complexes multiprotéiques (métabolisme), Cyclines (métabolisme), Cytométrie en flux (MeSH), Immunoprécipitation (MeSH), Immunotransfert (MeSH), Kinases cyclines-dépendantes (métabolisme), Mitogen-Activated Protein Kinases (métabolisme), Peptides (MeSH), Phosphorylation (MeSH), Points de contrôle de la phase G1 du cycle cellulaire (MeSH), Protein Phosphatase 2 (métabolisme), Protein kinases (métabolisme), Protéines de Saccharomyces cerevisiae (métabolisme), Protéines du cycle cellulaire (métabolisme), Protéines et peptides de signalisation intercellulaire (MeSH), Protéines inhibitrices des kinases cyclines-dépendantes (métabolisme), Saccharomyces cerevisiae (MeSH), Sérine-thréonine kinases TOR (métabolisme), Technique de Northern (MeSH), Ubiquitin-protein ligase complexes (métabolisme).
- MESH :
- métabolisme : Complexes multiprotéiques, Cyclines, Kinases cyclines-dépendantes, Mitogen-Activated Protein Kinases, Protein Phosphatase 2, Protein kinases, Protéines de Saccharomyces cerevisiae, Protéines du cycle cellulaire, Protéines inhibitrices des kinases cyclines-dépendantes, Sérine-thréonine kinases TOR, Ubiquitin-protein ligase complexes.
- Complexe-1 cible mécanistique de la rapamycine, Cytométrie en flux, Immunoprécipitation, Immunotransfert, Peptides, Phosphorylation, Points de contrôle de la phase G1 du cycle cellulaire, Protéines et peptides de signalisation intercellulaire, Saccharomyces cerevisiae, Technique de Northern.
English descriptors
- KwdEn :
- Blotting, Northern (MeSH), Cell Cycle Proteins (metabolism), Cyclin-Dependent Kinase Inhibitor Proteins (metabolism), Cyclin-Dependent Kinases (metabolism), Cyclins (metabolism), Flow Cytometry (MeSH), G1 Phase Cell Cycle Checkpoints (MeSH), Immunoblotting (MeSH), Immunoprecipitation (MeSH), Intercellular Signaling Peptides and Proteins (MeSH), Mechanistic Target of Rapamycin Complex 1 (MeSH), Mitogen-Activated Protein Kinases (metabolism), Multiprotein Complexes (metabolism), Peptides (MeSH), Phosphorylation (MeSH), Protein Kinases (metabolism), Protein Phosphatase 2 (metabolism), Saccharomyces cerevisiae (MeSH), Saccharomyces cerevisiae Proteins (metabolism), TOR Serine-Threonine Kinases (metabolism), Ubiquitin-Protein Ligase Complexes (metabolism).
- MESH :
- chemical , metabolism : Cell Cycle Proteins, Cyclin-Dependent Kinase Inhibitor Proteins, Cyclin-Dependent Kinases, Cyclins, Mitogen-Activated Protein Kinases, Multiprotein Complexes, Protein Kinases, Protein Phosphatase 2, Saccharomyces cerevisiae Proteins, TOR Serine-Threonine Kinases, Ubiquitin-Protein Ligase Complexes.
- Blotting, Northern, Flow Cytometry, G1 Phase Cell Cycle Checkpoints, Immunoblotting, Immunoprecipitation, Intercellular Signaling Peptides and Proteins, Mechanistic Target of Rapamycin Complex 1, Peptides, Phosphorylation, Saccharomyces cerevisiae.
Abstract
The target of rapamycin complex 1 (TORC1) pathway couples nutrient, energy and hormonal signals with eukaryotic cell growth and division. In yeast, TORC1 coordinates growth with G1-S cell cycle progression, also coined as START, by favouring the expression of G1 cyclins that activate cyclin-dependent protein kinases (CDKs) and by destabilizing the CDK inhibitor Sic1. Following TORC1 downregulation by rapamycin treatment or nutrient limitation, clearance of G1 cyclins and C-terminal phosphorylation of Sic1 by unknown protein kinases are both required for Sic1 to escape ubiquitin-dependent proteolysis prompted by its flagging via the SCF(Cdc4) (Skp1/Cul1/F-box protein) ubiquitin ligase complex. Here we show that the stabilizing phosphorylation event within the C-terminus of Sic1 requires stimulation of the mitogen-activated protein kinase, Mpk1, and inhibition of the Cdc55 protein phosphatase 2A (PP2A(Cdc55)) by greatwall kinase-activated endosulfines. Thus, Mpk1 and the greatwall kinase pathway serve TORC1 to coordinate the phosphorylation status of Sic1 and consequently START with nutrient availability.
DOI: 10.1038/ncomms9256
PubMed: 26356805
PubMed Central: PMC4579850
Affiliations:
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(MeSH)</term><term>Phosphorylation (MeSH)</term><term>Protein Kinases (metabolism)</term><term>Protein Phosphatase 2 (metabolism)</term><term>Saccharomyces cerevisiae (MeSH)</term><term>Saccharomyces cerevisiae Proteins (metabolism)</term><term>TOR Serine-Threonine Kinases (metabolism)</term><term>Ubiquitin-Protein Ligase Complexes (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Complexe-1 cible mécanistique de la rapamycine (MeSH)</term><term>Complexes multiprotéiques (métabolisme)</term><term>Cyclines (métabolisme)</term><term>Cytométrie en flux (MeSH)</term><term>Immunoprécipitation (MeSH)</term><term>Immunotransfert (MeSH)</term><term>Kinases cyclines-dépendantes (métabolisme)</term><term>Mitogen-Activated Protein Kinases (métabolisme)</term><term>Peptides (MeSH)</term><term>Phosphorylation (MeSH)</term><term>Points de contrôle de la phase G1 du cycle cellulaire (MeSH)</term><term>Protein Phosphatase 2 (métabolisme)</term><term>Protein kinases (métabolisme)</term><term>Protéines de Saccharomyces cerevisiae (métabolisme)</term><term>Protéines du cycle cellulaire (métabolisme)</term><term>Protéines et peptides de signalisation intercellulaire (MeSH)</term><term>Protéines inhibitrices des kinases cyclines-dépendantes (métabolisme)</term><term>Saccharomyces cerevisiae (MeSH)</term><term>Sérine-thréonine kinases TOR (métabolisme)</term><term>Technique de Northern (MeSH)</term><term>Ubiquitin-protein ligase complexes (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cell Cycle Proteins</term><term>Cyclin-Dependent Kinase Inhibitor Proteins</term><term>Cyclin-Dependent Kinases</term><term>Cyclins</term><term>Mitogen-Activated Protein Kinases</term><term>Multiprotein Complexes</term><term>Protein Kinases</term><term>Protein Phosphatase 2</term><term>Saccharomyces cerevisiae Proteins</term><term>TOR Serine-Threonine Kinases</term><term>Ubiquitin-Protein Ligase 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xml:lang="fr"><term>Complexe-1 cible mécanistique de la rapamycine</term><term>Cytométrie en flux</term><term>Immunoprécipitation</term><term>Immunotransfert</term><term>Peptides</term><term>Phosphorylation</term><term>Points de contrôle de la phase G1 du cycle cellulaire</term><term>Protéines et peptides de signalisation intercellulaire</term><term>Saccharomyces cerevisiae</term><term>Technique de Northern</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The target of rapamycin complex 1 (TORC1) pathway couples nutrient, energy and hormonal signals with eukaryotic cell growth and division. In yeast, TORC1 coordinates growth with G1-S cell cycle progression, also coined as START, by favouring the expression of G1 cyclins that activate cyclin-dependent protein kinases (CDKs) and by destabilizing the CDK inhibitor Sic1. Following TORC1 downregulation by rapamycin treatment or nutrient limitation, clearance of G1 cyclins and C-terminal phosphorylation of Sic1 by unknown protein kinases are both required for Sic1 to escape ubiquitin-dependent proteolysis prompted by its flagging via the SCF(Cdc4) (Skp1/Cul1/F-box protein) ubiquitin ligase complex. Here we show that the stabilizing phosphorylation event within the C-terminus of Sic1 requires stimulation of the mitogen-activated protein kinase, Mpk1, and inhibition of the Cdc55 protein phosphatase 2A (PP2A(Cdc55)) by greatwall kinase-activated endosulfines. Thus, Mpk1 and the greatwall kinase pathway serve TORC1 to coordinate the phosphorylation status of Sic1 and consequently START with nutrient availability. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">26356805</PMID><DateCompleted><Year>2016</Year><Month>04</Month><Day>26</Day></DateCompleted><DateRevised><Year>2019</Year><Month>12</Month><Day>10</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">2041-1723</ISSN><JournalIssue CitedMedium="Internet"><Volume>6</Volume><PubDate><Year>2015</Year><Month>Sep</Month><Day>10</Day></PubDate></JournalIssue><Title>Nature communications</Title><ISOAbbreviation>Nat Commun</ISOAbbreviation></Journal><ArticleTitle>TORC1 controls G1-S cell cycle transition in yeast via Mpk1 and the greatwall kinase pathway.</ArticleTitle><Pagination><MedlinePgn>8256</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1038/ncomms9256</ELocationID><Abstract><AbstractText>The target of rapamycin complex 1 (TORC1) pathway couples nutrient, energy and hormonal signals with eukaryotic cell growth and division. In yeast, TORC1 coordinates growth with G1-S cell cycle progression, also coined as START, by favouring the expression of G1 cyclins that activate cyclin-dependent protein kinases (CDKs) and by destabilizing the CDK inhibitor Sic1. Following TORC1 downregulation by rapamycin treatment or nutrient limitation, clearance of G1 cyclins and C-terminal phosphorylation of Sic1 by unknown protein kinases are both required for Sic1 to escape ubiquitin-dependent proteolysis prompted by its flagging via the SCF(Cdc4) (Skp1/Cul1/F-box protein) ubiquitin ligase complex. Here we show that the stabilizing phosphorylation event within the C-terminus of Sic1 requires stimulation of the mitogen-activated protein kinase, Mpk1, and inhibition of the Cdc55 protein phosphatase 2A (PP2A(Cdc55)) by greatwall kinase-activated endosulfines. Thus, Mpk1 and the greatwall kinase pathway serve TORC1 to coordinate the phosphorylation status of Sic1 and consequently START with nutrient availability. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Moreno-Torres</LastName><ForeName>Marta</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Department of Biology, University of Fribourg, Chemin du Musée 10, Fribourg CH-1700, Switzerland.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Jaquenoud</LastName><ForeName>Malika</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Department of Biology, University of Fribourg, Chemin du Musée 10, Fribourg CH-1700, Switzerland.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>De Virgilio</LastName><ForeName>Claudio</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Department of Biology, University of Fribourg, Chemin du Musée 10, Fribourg CH-1700, Switzerland.</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>2015</Year><Month>09</Month><Day>10</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Nat Commun</MedlineTA><NlmUniqueID>101528555</NlmUniqueID><ISSNLinking>2041-1723</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C071246">CDC55 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018797">Cell Cycle Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D050756">Cyclin-Dependent Kinase Inhibitor 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UI="C072724">SLT2 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.1.3.16</RegistryNumber><NameOfSubstance UI="D054648">Protein Phosphatase 2</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D015152" MajorTopicYN="N">Blotting, Northern</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018797" MajorTopicYN="N">Cell Cycle Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D050756" MajorTopicYN="N">Cyclin-Dependent Kinase Inhibitor Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018844" MajorTopicYN="N">Cyclin-Dependent Kinases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016213" 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MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D046912" MajorTopicYN="N">Multiprotein Complexes</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010455" MajorTopicYN="N">Peptides</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010766" MajorTopicYN="N">Phosphorylation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011494" MajorTopicYN="N">Protein Kinases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054648" MajorTopicYN="N">Protein Phosphatase 2</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D029701" MajorTopicYN="N">Saccharomyces cerevisiae 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Fribourg"><name sortKey="Moreno Torres, Marta" sort="Moreno Torres, Marta" uniqKey="Moreno Torres M" first="Marta" last="Moreno-Torres">Marta Moreno-Torres</name></region><name sortKey="De Virgilio, Claudio" sort="De Virgilio, Claudio" uniqKey="De Virgilio C" first="Claudio" last="De Virgilio">Claudio De Virgilio</name><name sortKey="Jaquenoud, Malika" sort="Jaquenoud, Malika" uniqKey="Jaquenoud M" first="Malika" last="Jaquenoud">Malika Jaquenoud</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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