The rapamycin-sensitive phosphoproteome reveals that TOR controls protein kinase A toward some but not all substrates.
Identifieur interne : 001377 ( Main/Exploration ); précédent : 001376; suivant : 001378The rapamycin-sensitive phosphoproteome reveals that TOR controls protein kinase A toward some but not all substrates.
Auteurs : Alexandre Soulard [Suisse] ; Alessio Cremonesi ; Suzette Moes ; Frédéric Schütz ; Paul Jenö ; Michael N. HallSource :
- Molecular biology of the cell [ 1939-4586 ] ; 2010.
Descripteurs français
- KwdFr :
- Activation enzymatique (effets des médicaments et des substances chimiques), Cyclic AMP-Dependent Protein Kinases (métabolisme), Données de séquences moléculaires (MeSH), Facteurs de transcription (métabolisme), Marquage isotopique (MeSH), Phosphopeptides (composition chimique), Phosphopeptides (métabolisme), Phosphoprotéines (métabolisme), Phosphorylation (effets des médicaments et des substances chimiques), Phosphothréonine (métabolisme), Protéines de Saccharomyces cerevisiae (antagonistes et inhibiteurs), Protéines de Saccharomyces cerevisiae (métabolisme), Protéome (métabolisme), Saccharomyces cerevisiae (effets des médicaments et des substances chimiques), Saccharomyces cerevisiae (enzymologie), Sirolimus (pharmacologie), Spécificité du substrat (effets des médicaments et des substances chimiques), Séquence d'acides aminés (MeSH), Sérine-thréonine kinases TOR (antagonistes et inhibiteurs), Sérine-thréonine kinases TOR (métabolisme).
- MESH :
- antagonistes et inhibiteurs : Protéines de Saccharomyces cerevisiae, Sérine-thréonine kinases TOR.
- composition chimique : Phosphopeptides.
- effets des médicaments et des substances chimiques : Activation enzymatique, Phosphorylation, Saccharomyces cerevisiae, Spécificité du substrat.
- enzymologie : Saccharomyces cerevisiae.
- métabolisme : Cyclic AMP-Dependent Protein Kinases, Facteurs de transcription, Phosphopeptides, Phosphoprotéines, Phosphothréonine, Protéines de Saccharomyces cerevisiae, Protéome, Sérine-thréonine kinases TOR.
- pharmacologie : Sirolimus.
- Données de séquences moléculaires, Marquage isotopique, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Cyclic AMP-Dependent Protein Kinases (metabolism), Enzyme Activation (drug effects), Isotope Labeling (MeSH), Molecular Sequence Data (MeSH), Phosphopeptides (chemistry), Phosphopeptides (metabolism), Phosphoproteins (metabolism), Phosphorylation (drug effects), Phosphothreonine (metabolism), Proteome (metabolism), Saccharomyces cerevisiae (drug effects), Saccharomyces cerevisiae (enzymology), Saccharomyces cerevisiae Proteins (antagonists & inhibitors), Saccharomyces cerevisiae Proteins (metabolism), Sirolimus (pharmacology), Substrate Specificity (drug effects), TOR Serine-Threonine Kinases (antagonists & inhibitors), TOR Serine-Threonine Kinases (metabolism), Transcription Factors (metabolism).
- MESH :
- chemical , antagonists & inhibitors : Saccharomyces cerevisiae Proteins, TOR Serine-Threonine Kinases.
- chemical , chemistry : Phosphopeptides.
- chemical , metabolism : Cyclic AMP-Dependent Protein Kinases, Phosphopeptides, Phosphoproteins, Phosphothreonine, Proteome, Saccharomyces cerevisiae Proteins, TOR Serine-Threonine Kinases, Transcription Factors.
- drug effects : Enzyme Activation, Phosphorylation, Saccharomyces cerevisiae, Substrate Specificity.
- enzymology : Saccharomyces cerevisiae.
- chemical , pharmacology : Sirolimus.
- Amino Acid Sequence, Isotope Labeling, Molecular Sequence Data.
Abstract
Regulation of cell growth requires extensive coordination of several processes including transcription, ribosome biogenesis, translation, nutrient metabolism, and autophagy. In yeast, the protein kinases Target of Rapamycin (TOR) and protein kinase A (PKA) regulate these processes and are thereby the main activators of cell growth in response to nutrients. How TOR, PKA, and their corresponding signaling pathways are coordinated to control the same cellular processes is not understood. Quantitative analysis of the rapamycin-sensitive phosphoproteome combined with targeted analysis of PKA substrates suggests that TOR complex 1 (TORC1) activates PKA but only toward a subset of substrates. Furthermore, we show that TORC1 signaling impinges on BCY1, the negative regulatory subunit of PKA. Inhibition of TORC1 with rapamycin leads to BCY1 phosphorylation on several sites including T129. Phosphorylation of BCY1 T129 results in BCY1 activation and inhibition of PKA. TORC1 inhibits BCY1 T129 phosphorylation by phosphorylating and activating the S6K homolog SCH9 that in turn inhibits the MAP kinase MPK1. MPK1 phosphorylates BCY1 T129 directly. Thus, TORC1 activates PKA toward some substrates by preventing MPK1-mediated activation of BCY1.
DOI: 10.1091/mbc.E10-03-0182
PubMed: 20702584
PubMed Central: PMC2947482
Affiliations:
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xml:lang="fr"><term>Données de séquences moléculaires</term><term>Marquage isotopique</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Regulation of cell growth requires extensive coordination of several processes including transcription, ribosome biogenesis, translation, nutrient metabolism, and autophagy. In yeast, the protein kinases Target of Rapamycin (TOR) and protein kinase A (PKA) regulate these processes and are thereby the main activators of cell growth in response to nutrients. How TOR, PKA, and their corresponding signaling pathways are coordinated to control the same cellular processes is not understood. Quantitative analysis of the rapamycin-sensitive phosphoproteome combined with targeted analysis of PKA substrates suggests that TOR complex 1 (TORC1) activates PKA but only toward a subset of substrates. Furthermore, we show that TORC1 signaling impinges on BCY1, the negative regulatory subunit of PKA. Inhibition of TORC1 with rapamycin leads to BCY1 phosphorylation on several sites including T129. Phosphorylation of BCY1 T129 results in BCY1 activation and inhibition of PKA. TORC1 inhibits BCY1 T129 phosphorylation by phosphorylating and activating the S6K homolog SCH9 that in turn inhibits the MAP kinase MPK1. MPK1 phosphorylates BCY1 T129 directly. Thus, TORC1 activates PKA toward some substrates by preventing MPK1-mediated activation of BCY1.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">20702584</PMID><DateCompleted><Year>2011</Year><Month>01</Month><Day>18</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1939-4586</ISSN><JournalIssue CitedMedium="Internet"><Volume>21</Volume><Issue>19</Issue><PubDate><Year>2010</Year><Month>Oct</Month><Day>01</Day></PubDate></JournalIssue><Title>Molecular biology of the cell</Title><ISOAbbreviation>Mol Biol Cell</ISOAbbreviation></Journal><ArticleTitle>The rapamycin-sensitive phosphoproteome reveals that TOR controls protein kinase A toward some but not all substrates.</ArticleTitle><Pagination><MedlinePgn>3475-86</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1091/mbc.E10-03-0182</ELocationID><Abstract><AbstractText>Regulation of cell growth requires extensive coordination of several processes including transcription, ribosome biogenesis, translation, nutrient metabolism, and autophagy. In yeast, the protein kinases Target of Rapamycin (TOR) and protein kinase A (PKA) regulate these processes and are thereby the main activators of cell growth in response to nutrients. How TOR, PKA, and their corresponding signaling pathways are coordinated to control the same cellular processes is not understood. Quantitative analysis of the rapamycin-sensitive phosphoproteome combined with targeted analysis of PKA substrates suggests that TOR complex 1 (TORC1) activates PKA but only toward a subset of substrates. Furthermore, we show that TORC1 signaling impinges on BCY1, the negative regulatory subunit of PKA. Inhibition of TORC1 with rapamycin leads to BCY1 phosphorylation on several sites including T129. Phosphorylation of BCY1 T129 results in BCY1 activation and inhibition of PKA. TORC1 inhibits BCY1 T129 phosphorylation by phosphorylating and activating the S6K homolog SCH9 that in turn inhibits the MAP kinase MPK1. MPK1 phosphorylates BCY1 T129 directly. Thus, TORC1 activates PKA toward some substrates by preventing MPK1-mediated activation of BCY1.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Soulard</LastName><ForeName>Alexandre</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Biozentrum, University of Basel, CH-4056 Basel, Switzerland.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Cremonesi</LastName><ForeName>Alessio</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Moes</LastName><ForeName>Suzette</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Schütz</LastName><ForeName>Frédéric</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Jenö</LastName><ForeName>Paul</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Hall</LastName><ForeName>Michael N</ForeName><Initials>MN</Initials></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>2010</Year><Month>08</Month><Day>11</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="D010748">Phosphopeptides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010750">Phosphoproteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D020543">Proteome</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029701">Saccharomyces cerevisiae Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014157">Transcription Factors</NameOfSubstance></Chemical><Chemical><RegistryNumber>1114-81-4</RegistryNumber><NameOfSubstance UI="D010769">Phosphothreonine</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.1.1</RegistryNumber><NameOfSubstance UI="D058570">TOR Serine-Threonine Kinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.11</RegistryNumber><NameOfSubstance UI="D017868">Cyclic AMP-Dependent Protein Kinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>W36ZG6FT64</RegistryNumber><NameOfSubstance UI="D020123">Sirolimus</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017868" MajorTopicYN="N">Cyclic AMP-Dependent Protein Kinases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004789" MajorTopicYN="N">Enzyme Activation</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007553" MajorTopicYN="N">Isotope Labeling</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010748" MajorTopicYN="N">Phosphopeptides</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010750" MajorTopicYN="N">Phosphoproteins</DescriptorName><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="D010769" MajorTopicYN="N">Phosphothreonine</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020543" MajorTopicYN="N">Proteome</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029701" MajorTopicYN="N">Saccharomyces cerevisiae Proteins</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020123" MajorTopicYN="N">Sirolimus</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D058570" MajorTopicYN="N">TOR Serine-Threonine Kinases</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014157" MajorTopicYN="N">Transcription Factors</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2010</Year><Month>8</Month><Day>13</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate 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IdType="pubmed">15353587</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>Suisse</li></country></list><tree><noCountry><name sortKey="Cremonesi, Alessio" sort="Cremonesi, Alessio" uniqKey="Cremonesi A" first="Alessio" last="Cremonesi">Alessio Cremonesi</name><name sortKey="Hall, Michael N" sort="Hall, Michael N" uniqKey="Hall M" first="Michael N" last="Hall">Michael N. Hall</name><name sortKey="Jeno, Paul" sort="Jeno, Paul" uniqKey="Jeno P" first="Paul" last="Jenö">Paul Jenö</name><name sortKey="Moes, Suzette" sort="Moes, Suzette" uniqKey="Moes S" first="Suzette" last="Moes">Suzette Moes</name><name sortKey="Schutz, Frederic" sort="Schutz, Frederic" uniqKey="Schutz F" first="Frédéric" last="Schütz">Frédéric Schütz</name></noCountry><country name="Suisse"><noRegion><name sortKey="Soulard, Alexandre" sort="Soulard, Alexandre" uniqKey="Soulard A" first="Alexandre" last="Soulard">Alexandre Soulard</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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