TOR controls transcriptional and translational programs via Sap-Sit4 protein phosphatase signaling effectors.
Identifieur interne : 001871 ( Main/Exploration ); précédent : 001870; suivant : 001872TOR controls transcriptional and translational programs via Sap-Sit4 protein phosphatase signaling effectors.
Auteurs : John R. Rohde [États-Unis] ; Susan Campbell ; Sara A. Zurita-Martinez ; N Shane Cutler ; Mark Ashe ; Maria E. CardenasSource :
- Molecular and cellular biology [ 0270-7306 ] ; 2004.
Descripteurs français
- KwdFr :
- Biosynthèse des protéines (physiologie), Gènes rapporteurs (MeSH), Petites ribonucléoprotéines nucléaires U2 (génétique), Petites ribonucléoprotéines nucléaires U2 (métabolisme), Phosphatidylinositol 3-kinases (métabolisme), Phosphoprotein Phosphatases (métabolisme), Phosphoprotéines (génétique), Phosphoprotéines (métabolisme), Phosphotransferases (Alcohol Group Acceptor) (métabolisme), Protein Phosphatase 2 (MeSH), Protein kinases (métabolisme), Protein-Serine-Threonine Kinases (MeSH), Protéines adaptatrices de la transduction du signal (MeSH), Protéines de Saccharomyces cerevisiae (métabolisme), Régulation de l'expression des gènes (physiologie), Saccharomyces cerevisiae (enzymologie), Saccharomyces cerevisiae (métabolisme), Transcription génétique (physiologie), Transduction du signal (physiologie).
- MESH :
- enzymologie : Saccharomyces cerevisiae.
- génétique : Petites ribonucléoprotéines nucléaires U2, Phosphoprotéines.
- métabolisme : Petites ribonucléoprotéines nucléaires U2, Phosphatidylinositol 3-kinases, Phosphoprotein Phosphatases, Phosphoprotéines, Phosphotransferases (Alcohol Group Acceptor), Protein kinases, Protéines de Saccharomyces cerevisiae, Saccharomyces cerevisiae.
- physiologie : Biosynthèse des protéines, Régulation de l'expression des gènes, Transcription génétique, Transduction du signal.
- Gènes rapporteurs, Protein Phosphatase 2, Protein-Serine-Threonine Kinases, Protéines adaptatrices de la transduction du signal.
English descriptors
- KwdEn :
- Adaptor Proteins, Signal Transducing (MeSH), Gene Expression Regulation (physiology), Genes, Reporter (MeSH), Phosphatidylinositol 3-Kinases (metabolism), Phosphoprotein Phosphatases (metabolism), Phosphoproteins (genetics), Phosphoproteins (metabolism), Phosphotransferases (Alcohol Group Acceptor) (metabolism), Protein Biosynthesis (physiology), Protein Kinases (metabolism), Protein Phosphatase 2 (MeSH), Protein-Serine-Threonine Kinases (MeSH), Ribonucleoprotein, U2 Small Nuclear (genetics), Ribonucleoprotein, U2 Small Nuclear (metabolism), Saccharomyces cerevisiae (enzymology), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (metabolism), Signal Transduction (physiology), Transcription, Genetic (physiology).
- MESH :
- chemical , genetics : Phosphoproteins, Ribonucleoprotein, U2 Small Nuclear.
- chemical , metabolism : Phosphatidylinositol 3-Kinases, Phosphoprotein Phosphatases, Phosphoproteins, Phosphotransferases (Alcohol Group Acceptor), Protein Kinases, Ribonucleoprotein, U2 Small Nuclear, Saccharomyces cerevisiae Proteins.
- chemical : Adaptor Proteins, Signal Transducing, Protein Phosphatase 2, Protein-Serine-Threonine Kinases.
- enzymology : Saccharomyces cerevisiae.
- metabolism : Saccharomyces cerevisiae.
- physiology : Gene Expression Regulation, Protein Biosynthesis, Signal Transduction, Transcription, Genetic.
- Genes, Reporter.
Abstract
The Tor kinases are the targets of the immunosuppressive drug rapamycin and couple nutrient availability to cell growth. In the budding yeast Saccharomyces cerevisiae, the PP2A-related phosphatase Sit4 together with its regulatory subunit Tap42 mediates several Tor signaling events. Sit4 interacts with other potential regulatory proteins known as the Saps. Deletion of the SAP or SIT4 genes confers increased sensitivity to rapamycin and defects in expression of subsets of Tor-regulated genes. Sap155, Sap185, or Sap190 can restore these responses. Strains lacking Sap185 and Sap190 are hypersensitive to rapamycin, and this sensitivity is Gcn2 dependent and correlated with a defect in translation, constitutive eukaryotic initiation factor 2alpha hyperphosphorylation, induction of GCN4 translation, and hypersensitivity to amino acid starvation. We conclude that Tor signals via Sap-Sit4 complexes to control both transcriptional and translational programs that couple cell growth to amino acid availability.
DOI: 10.1128/MCB.24.19.8332-8341.2004
PubMed: 15367655
PubMed Central: PMC516738
Affiliations:
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Le document en format XML
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In the budding yeast Saccharomyces cerevisiae, the PP2A-related phosphatase Sit4 together with its regulatory subunit Tap42 mediates several Tor signaling events. Sit4 interacts with other potential regulatory proteins known as the Saps. Deletion of the SAP or SIT4 genes confers increased sensitivity to rapamycin and defects in expression of subsets of Tor-regulated genes. Sap155, Sap185, or Sap190 can restore these responses. Strains lacking Sap185 and Sap190 are hypersensitive to rapamycin, and this sensitivity is Gcn2 dependent and correlated with a defect in translation, constitutive eukaryotic initiation factor 2alpha hyperphosphorylation, induction of GCN4 translation, and hypersensitivity to amino acid starvation. We conclude that Tor signals via Sap-Sit4 complexes to control both transcriptional and translational programs that couple cell growth to amino acid availability.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15367655</PMID><DateCompleted><Year>2004</Year><Month>11</Month><Day>01</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0270-7306</ISSN><JournalIssue CitedMedium="Print"><Volume>24</Volume><Issue>19</Issue><PubDate><Year>2004</Year><Month>Oct</Month></PubDate></JournalIssue><Title>Molecular and cellular biology</Title><ISOAbbreviation>Mol Cell Biol</ISOAbbreviation></Journal><ArticleTitle>TOR controls transcriptional and translational programs via Sap-Sit4 protein phosphatase signaling effectors.</ArticleTitle><Pagination><MedlinePgn>8332-41</MedlinePgn></Pagination><Abstract><AbstractText>The Tor kinases are the targets of the immunosuppressive drug rapamycin and couple nutrient availability to cell growth. In the budding yeast Saccharomyces cerevisiae, the PP2A-related phosphatase Sit4 together with its regulatory subunit Tap42 mediates several Tor signaling events. Sit4 interacts with other potential regulatory proteins known as the Saps. Deletion of the SAP or SIT4 genes confers increased sensitivity to rapamycin and defects in expression of subsets of Tor-regulated genes. Sap155, Sap185, or Sap190 can restore these responses. Strains lacking Sap185 and Sap190 are hypersensitive to rapamycin, and this sensitivity is Gcn2 dependent and correlated with a defect in translation, constitutive eukaryotic initiation factor 2alpha hyperphosphorylation, induction of GCN4 translation, and hypersensitivity to amino acid starvation. We conclude that Tor signals via Sap-Sit4 complexes to control both transcriptional and translational programs that couple cell growth to amino acid availability.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Rohde</LastName><ForeName>John R</ForeName><Initials>JR</Initials><AffiliationInfo><Affiliation>Department of Molecular Genetics and Microbiology, Duke University Medical Center, 322 CARL Bldg., Box 3546, Research Dr., Durham, NC 27710, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Campbell</LastName><ForeName>Susan</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Zurita-Martinez</LastName><ForeName>Sara A</ForeName><Initials>SA</Initials></Author><Author ValidYN="Y"><LastName>Cutler</LastName><ForeName>N Shane</ForeName><Initials>NS</Initials></Author><Author ValidYN="Y"><LastName>Ashe</LastName><ForeName>Mark</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Cardenas</LastName><ForeName>Maria E</ForeName><Initials>ME</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>K22 CA094925</GrantID><Acronym>CA</Acronym><Agency>NCI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 CA114107</GrantID><Acronym>CA</Acronym><Agency>NCI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>K22 CA94925-01</GrantID><Acronym>CA</Acronym><Agency>NCI NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D013487">Research Support, U.S. Gov't, P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Mol Cell Biol</MedlineTA><NlmUniqueID>8109087</NlmUniqueID><ISSNLinking>0270-7306</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D048868">Adaptor Proteins, Signal Transducing</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010750">Phosphoproteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D017413">Ribonucleoprotein, U2 Small Nuclear</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C491800">SAP155 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029701">Saccharomyces cerevisiae Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.-</RegistryNumber><NameOfSubstance UI="D011494">Protein Kinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.1.-</RegistryNumber><NameOfSubstance UI="D019869">Phosphatidylinositol 3-Kinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.1.-</RegistryNumber><NameOfSubstance UI="D017853">Phosphotransferases (Alcohol Group Acceptor)</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.1.137</RegistryNumber><NameOfSubstance UI="C083324">TOR1 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber><NameOfSubstance UI="C512912">GCN2 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber><NameOfSubstance UI="D017346">Protein-Serine-Threonine Kinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.1.3.16</RegistryNumber><NameOfSubstance UI="D010749">Phosphoprotein Phosphatases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.1.3.16</RegistryNumber><NameOfSubstance UI="D054648">Protein Phosphatase 2</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.1.3.16</RegistryNumber><NameOfSubstance UI="C104343">SIT4 protein, S cerevisiae</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D048868" MajorTopicYN="N">Adaptor Proteins, Signal Transducing</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005786" MajorTopicYN="N">Gene Expression Regulation</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017930" MajorTopicYN="N">Genes, Reporter</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019869" MajorTopicYN="N">Phosphatidylinositol 3-Kinases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010749" MajorTopicYN="N">Phosphoprotein Phosphatases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010750" MajorTopicYN="N">Phosphoproteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017853" MajorTopicYN="N">Phosphotransferases (Alcohol Group Acceptor)</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014176" MajorTopicYN="N">Protein Biosynthesis</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011494" MajorTopicYN="N">Protein Kinases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054648" MajorTopicYN="N">Protein Phosphatase 2</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017346" MajorTopicYN="N">Protein-Serine-Threonine Kinases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017413" MajorTopicYN="N">Ribonucleoprotein, U2 Small Nuclear</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="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029701" MajorTopicYN="N">Saccharomyces cerevisiae Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015398" MajorTopicYN="N">Signal Transduction</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014158" 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Cardenas</name><name sortKey="Cutler, N Shane" sort="Cutler, N Shane" uniqKey="Cutler N" first="N Shane" last="Cutler">N Shane Cutler</name><name sortKey="Zurita Martinez, Sara A" sort="Zurita Martinez, Sara A" uniqKey="Zurita Martinez S" first="Sara A" last="Zurita-Martinez">Sara A. Zurita-Martinez</name></noCountry><country name="États-Unis"><region name="Caroline du Nord"><name sortKey="Rohde, John R" sort="Rohde, John R" uniqKey="Rohde J" first="John R" last="Rohde">John R. Rohde</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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