The TOR-controlled transcription activators GLN3, RTG1, and RTG3 are regulated in response to intracellular levels of glutamine.
Identifieur interne : 001964 ( Main/Exploration ); précédent : 001963; suivant : 001965The TOR-controlled transcription activators GLN3, RTG1, and RTG3 are regulated in response to intracellular levels of glutamine.
Auteurs : José L. Crespo [Suisse] ; Ted Powers ; Brian Fowler ; Michael N. HallSource :
- Proceedings of the National Academy of Sciences of the United States of America [ 0027-8424 ] ; 2002.
Descripteurs français
- KwdFr :
- Acide glutamique (métabolisme), Antienzymes (pharmacologie), Expression des gènes (MeSH), Facteurs de transcription (MeSH), Facteurs de transcription à motifs basiques hélice-boucle-hélice et à glissière à leucines (MeSH), Glutamate-ammonia ligase (antagonistes et inhibiteurs), Glutamine (métabolisme), Liquide intracellulaire (métabolisme), Méthionine sulfoximine (pharmacologie), Phosphatidylinositol 3-kinases (MeSH), Phosphotransferases (Alcohol Group Acceptor) (génétique), Phosphotransferases (Alcohol Group Acceptor) (métabolisme), Protéines de Saccharomyces cerevisiae (MeSH), Protéines de liaison à l'ADN (métabolisme), Protéines de répression (MeSH), Protéines de transport (génétique), Protéines fongiques (génétique), Protéines fongiques (métabolisme), Saccharomyces cerevisiae (croissance et développement), Saccharomyces cerevisiae (effets des médicaments et des substances chimiques), Saccharomyces cerevisiae (métabolisme), Transactivateurs (métabolisme), Transduction du signal (MeSH), Transporteurs de cations (MeSH).
- MESH :
- antagonistes et inhibiteurs : Glutamate-ammonia ligase.
- croissance et développement : Saccharomyces cerevisiae.
- effets des médicaments et des substances chimiques : Saccharomyces cerevisiae.
- génétique : Phosphotransferases (Alcohol Group Acceptor), Protéines de transport, Protéines fongiques.
- métabolisme : Acide glutamique, Glutamine, Liquide intracellulaire, Phosphotransferases (Alcohol Group Acceptor), Protéines de liaison à l'ADN, Protéines fongiques, Saccharomyces cerevisiae, Transactivateurs.
- pharmacologie : Antienzymes, Méthionine sulfoximine.
- Expression des gènes, Facteurs de transcription, Facteurs de transcription à motifs basiques hélice-boucle-hélice et à glissière à leucines, Phosphatidylinositol 3-kinases, Protéines de Saccharomyces cerevisiae, Protéines de répression, Transduction du signal, Transporteurs de cations.
English descriptors
- KwdEn :
- Basic Helix-Loop-Helix Leucine Zipper Transcription Factors (MeSH), Carrier Proteins (genetics), Cation Transport Proteins (MeSH), DNA-Binding Proteins (metabolism), Enzyme Inhibitors (pharmacology), Fungal Proteins (genetics), Fungal Proteins (metabolism), Gene Expression (MeSH), Glutamate-Ammonia Ligase (antagonists & inhibitors), Glutamic Acid (metabolism), Glutamine (metabolism), Intracellular Fluid (metabolism), Methionine Sulfoximine (pharmacology), Phosphatidylinositol 3-Kinases (MeSH), Phosphotransferases (Alcohol Group Acceptor) (genetics), Phosphotransferases (Alcohol Group Acceptor) (metabolism), Repressor Proteins (MeSH), Saccharomyces cerevisiae (drug effects), Saccharomyces cerevisiae (growth & development), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (MeSH), Signal Transduction (MeSH), Trans-Activators (metabolism), Transcription Factors (MeSH).
- MESH :
- chemical , antagonists & inhibitors : Glutamate-Ammonia Ligase.
- chemical , genetics : Carrier Proteins, Fungal Proteins, Phosphotransferases (Alcohol Group Acceptor).
- chemical , metabolism : DNA-Binding Proteins, Fungal Proteins, Glutamic Acid, Glutamine, Phosphotransferases (Alcohol Group Acceptor), Trans-Activators.
- chemical , pharmacology : Enzyme Inhibitors, Methionine Sulfoximine.
- chemical : Basic Helix-Loop-Helix Leucine Zipper Transcription Factors, Cation Transport Proteins, Phosphatidylinositol 3-Kinases, Repressor Proteins, Saccharomyces cerevisiae Proteins, Transcription Factors.
- drug effects : Saccharomyces cerevisiae.
- growth & development : Saccharomyces cerevisiae.
- metabolism : Intracellular Fluid, Saccharomyces cerevisiae.
- Gene Expression, Signal Transduction.
Abstract
The essential, rapamycin-sensitive TOR kinases regulate a diverse set of cell growth-related readouts in response to nutrients. Thus, the yeast TOR proteins function as nutrient sensors, in particular as sensors of nitrogen and possibly carbon. However, the nutrient metabolite(s) that acts upstream of TOR is unknown. We investigated the role of glutamine, a preferred nitrogen source and a key intermediate in yeast nitrogen metabolism, as a possible regulator of TOR. We show that the glutamine synthetase inhibitor L-methionine sulfoximine (MSX) specifically provokes glutamine depletion in yeast cells. MSX-induced glutamine starvation caused nuclear localization and activation of the TOR-inhibited transcription factors GLN3, RTG1, and RTG3, all of which mediate glutamine synthesis. The MSX-induced nuclear localization of GLN3 required the TOR-controlled, type 2A-related phosphatase SIT4. Other TOR-controlled transcription factors, GAT1/NIL1, MSN2, MSN4, and an unknown factor involved in the expression of ribosomal protein genes, were not affected by glutamine starvation. These findings suggest that the TOR pathway senses glutamine. Furthermore, as glutamine starvation affects only a subset of TOR-controlled transcription factors, TOR appears to discriminate between different nutrient conditions to elicit a response appropriate to a given condition.
DOI: 10.1073/pnas.102687599
PubMed: 11997479
PubMed Central: PMC124480
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">The TOR-controlled transcription activators GLN3, RTG1, and RTG3 are regulated in response to intracellular levels of glutamine.</title><author><name sortKey="Crespo, Jose L" sort="Crespo, Jose L" uniqKey="Crespo J" first="José L" last="Crespo">José L. Crespo</name><affiliation wicri:level="1"><nlm:affiliation>Division of Biochemistry, Biozentrum, University of Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland.</nlm:affiliation><country xml:lang="fr">Suisse</country><wicri:regionArea>Division of Biochemistry, Biozentrum, University of Basel, Klingelbergstrasse 70, CH-4056 Basel</wicri:regionArea><wicri:noRegion>CH-4056 Basel</wicri:noRegion></affiliation></author><author><name sortKey="Powers, Ted" sort="Powers, Ted" uniqKey="Powers T" first="Ted" last="Powers">Ted Powers</name></author><author><name sortKey="Fowler, Brian" sort="Fowler, Brian" uniqKey="Fowler B" first="Brian" last="Fowler">Brian Fowler</name></author><author><name sortKey="Hall, Michael N" sort="Hall, Michael N" uniqKey="Hall M" first="Michael N" last="Hall">Michael N. Hall</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2002">2002</date><idno type="RBID">pubmed:11997479</idno><idno type="pmid">11997479</idno><idno type="doi">10.1073/pnas.102687599</idno><idno type="pmc">PMC124480</idno><idno type="wicri:Area/Main/Corpus">001977</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">001977</idno><idno type="wicri:Area/Main/Curation">001977</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">001977</idno><idno type="wicri:Area/Main/Exploration">001977</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">The TOR-controlled transcription activators GLN3, RTG1, and RTG3 are regulated in response to intracellular levels of glutamine.</title><author><name sortKey="Crespo, Jose L" sort="Crespo, Jose L" uniqKey="Crespo J" first="José L" last="Crespo">José L. Crespo</name><affiliation wicri:level="1"><nlm:affiliation>Division of Biochemistry, Biozentrum, University of Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland.</nlm:affiliation><country xml:lang="fr">Suisse</country><wicri:regionArea>Division of Biochemistry, Biozentrum, University of Basel, Klingelbergstrasse 70, CH-4056 Basel</wicri:regionArea><wicri:noRegion>CH-4056 Basel</wicri:noRegion></affiliation></author><author><name sortKey="Powers, Ted" sort="Powers, Ted" uniqKey="Powers T" first="Ted" last="Powers">Ted Powers</name></author><author><name sortKey="Fowler, Brian" sort="Fowler, Brian" uniqKey="Fowler B" first="Brian" last="Fowler">Brian Fowler</name></author><author><name sortKey="Hall, Michael N" sort="Hall, Michael N" uniqKey="Hall M" first="Michael N" last="Hall">Michael N. Hall</name></author></analytic><series><title level="j">Proceedings of the National Academy of Sciences of the United States of America</title><idno type="ISSN">0027-8424</idno><imprint><date when="2002" type="published">2002</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Basic Helix-Loop-Helix Leucine Zipper Transcription Factors (MeSH)</term><term>Carrier Proteins (genetics)</term><term>Cation Transport Proteins (MeSH)</term><term>DNA-Binding Proteins (metabolism)</term><term>Enzyme Inhibitors (pharmacology)</term><term>Fungal Proteins (genetics)</term><term>Fungal Proteins (metabolism)</term><term>Gene Expression (MeSH)</term><term>Glutamate-Ammonia Ligase (antagonists & inhibitors)</term><term>Glutamic Acid (metabolism)</term><term>Glutamine (metabolism)</term><term>Intracellular Fluid (metabolism)</term><term>Methionine Sulfoximine (pharmacology)</term><term>Phosphatidylinositol 3-Kinases (MeSH)</term><term>Phosphotransferases (Alcohol Group Acceptor) (genetics)</term><term>Phosphotransferases (Alcohol Group Acceptor) (metabolism)</term><term>Repressor Proteins (MeSH)</term><term>Saccharomyces cerevisiae (drug effects)</term><term>Saccharomyces cerevisiae (growth & development)</term><term>Saccharomyces cerevisiae (metabolism)</term><term>Saccharomyces cerevisiae Proteins (MeSH)</term><term>Signal Transduction (MeSH)</term><term>Trans-Activators (metabolism)</term><term>Transcription Factors (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acide glutamique (métabolisme)</term><term>Antienzymes (pharmacologie)</term><term>Expression des gènes (MeSH)</term><term>Facteurs de transcription (MeSH)</term><term>Facteurs de transcription à motifs basiques hélice-boucle-hélice et à glissière à leucines (MeSH)</term><term>Glutamate-ammonia ligase (antagonistes et inhibiteurs)</term><term>Glutamine (métabolisme)</term><term>Liquide intracellulaire (métabolisme)</term><term>Méthionine sulfoximine (pharmacologie)</term><term>Phosphatidylinositol 3-kinases (MeSH)</term><term>Phosphotransferases (Alcohol Group Acceptor) (génétique)</term><term>Phosphotransferases (Alcohol Group Acceptor) (métabolisme)</term><term>Protéines de Saccharomyces cerevisiae (MeSH)</term><term>Protéines de liaison à l'ADN (métabolisme)</term><term>Protéines de répression (MeSH)</term><term>Protéines de transport (génétique)</term><term>Protéines fongiques (génétique)</term><term>Protéines fongiques (métabolisme)</term><term>Saccharomyces cerevisiae (croissance et développement)</term><term>Saccharomyces cerevisiae (effets des médicaments et des substances chimiques)</term><term>Saccharomyces cerevisiae (métabolisme)</term><term>Transactivateurs (métabolisme)</term><term>Transduction du signal (MeSH)</term><term>Transporteurs de cations (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Glutamate-Ammonia Ligase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Carrier Proteins</term><term>Fungal Proteins</term><term>Phosphotransferases (Alcohol Group Acceptor)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>DNA-Binding Proteins</term><term>Fungal Proteins</term><term>Glutamic Acid</term><term>Glutamine</term><term>Phosphotransferases (Alcohol Group Acceptor)</term><term>Trans-Activators</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Enzyme Inhibitors</term><term>Methionine Sulfoximine</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Basic Helix-Loop-Helix Leucine Zipper Transcription Factors</term><term>Cation Transport Proteins</term><term>Phosphatidylinositol 3-Kinases</term><term>Repressor Proteins</term><term>Saccharomyces cerevisiae Proteins</term><term>Transcription Factors</term></keywords><keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Glutamate-ammonia ligase</term></keywords><keywords scheme="MESH" qualifier="croissance et développement" xml:lang="fr"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="growth & development" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Phosphotransferases (Alcohol Group Acceptor)</term><term>Protéines de transport</term><term>Protéines fongiques</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Intracellular Fluid</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Acide glutamique</term><term>Glutamine</term><term>Liquide intracellulaire</term><term>Phosphotransferases (Alcohol Group Acceptor)</term><term>Protéines de liaison à l'ADN</term><term>Protéines fongiques</term><term>Saccharomyces cerevisiae</term><term>Transactivateurs</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Antienzymes</term><term>Méthionine sulfoximine</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Gene Expression</term><term>Signal Transduction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Expression des gènes</term><term>Facteurs de transcription</term><term>Facteurs de transcription à motifs basiques hélice-boucle-hélice et à glissière à leucines</term><term>Phosphatidylinositol 3-kinases</term><term>Protéines de Saccharomyces cerevisiae</term><term>Protéines de répression</term><term>Transduction du signal</term><term>Transporteurs de cations</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The essential, rapamycin-sensitive TOR kinases regulate a diverse set of cell growth-related readouts in response to nutrients. Thus, the yeast TOR proteins function as nutrient sensors, in particular as sensors of nitrogen and possibly carbon. However, the nutrient metabolite(s) that acts upstream of TOR is unknown. We investigated the role of glutamine, a preferred nitrogen source and a key intermediate in yeast nitrogen metabolism, as a possible regulator of TOR. We show that the glutamine synthetase inhibitor L-methionine sulfoximine (MSX) specifically provokes glutamine depletion in yeast cells. MSX-induced glutamine starvation caused nuclear localization and activation of the TOR-inhibited transcription factors GLN3, RTG1, and RTG3, all of which mediate glutamine synthesis. The MSX-induced nuclear localization of GLN3 required the TOR-controlled, type 2A-related phosphatase SIT4. Other TOR-controlled transcription factors, GAT1/NIL1, MSN2, MSN4, and an unknown factor involved in the expression of ribosomal protein genes, were not affected by glutamine starvation. These findings suggest that the TOR pathway senses glutamine. Furthermore, as glutamine starvation affects only a subset of TOR-controlled transcription factors, TOR appears to discriminate between different nutrient conditions to elicit a response appropriate to a given condition.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">11997479</PMID><DateCompleted><Year>2002</Year><Month>06</Month><Day>18</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0027-8424</ISSN><JournalIssue CitedMedium="Print"><Volume>99</Volume><Issue>10</Issue><PubDate><Year>2002</Year><Month>May</Month><Day>14</Day></PubDate></JournalIssue><Title>Proceedings of the National Academy of Sciences of the United States of America</Title><ISOAbbreviation>Proc Natl Acad Sci U S A</ISOAbbreviation></Journal><ArticleTitle>The TOR-controlled transcription activators GLN3, RTG1, and RTG3 are regulated in response to intracellular levels of glutamine.</ArticleTitle><Pagination><MedlinePgn>6784-9</MedlinePgn></Pagination><Abstract><AbstractText>The essential, rapamycin-sensitive TOR kinases regulate a diverse set of cell growth-related readouts in response to nutrients. Thus, the yeast TOR proteins function as nutrient sensors, in particular as sensors of nitrogen and possibly carbon. However, the nutrient metabolite(s) that acts upstream of TOR is unknown. We investigated the role of glutamine, a preferred nitrogen source and a key intermediate in yeast nitrogen metabolism, as a possible regulator of TOR. We show that the glutamine synthetase inhibitor L-methionine sulfoximine (MSX) specifically provokes glutamine depletion in yeast cells. MSX-induced glutamine starvation caused nuclear localization and activation of the TOR-inhibited transcription factors GLN3, RTG1, and RTG3, all of which mediate glutamine synthesis. The MSX-induced nuclear localization of GLN3 required the TOR-controlled, type 2A-related phosphatase SIT4. Other TOR-controlled transcription factors, GAT1/NIL1, MSN2, MSN4, and an unknown factor involved in the expression of ribosomal protein genes, were not affected by glutamine starvation. These findings suggest that the TOR pathway senses glutamine. Furthermore, as glutamine starvation affects only a subset of TOR-controlled transcription factors, TOR appears to discriminate between different nutrient conditions to elicit a response appropriate to a given condition.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Crespo</LastName><ForeName>José L</ForeName><Initials>JL</Initials><AffiliationInfo><Affiliation>Division of Biochemistry, Biozentrum, University of Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Powers</LastName><ForeName>Ted</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Fowler</LastName><ForeName>Brian</ForeName><Initials>B</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>2002</Year><Month>05</Month><Day>07</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Proc Natl Acad Sci U S A</MedlineTA><NlmUniqueID>7505876</NlmUniqueID><ISSNLinking>0027-8424</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D051778">Basic Helix-Loop-Helix Leucine Zipper Transcription Factors</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D002352">Carrier Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D027682">Cation Transport Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004268">DNA-Binding Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004791">Enzyme Inhibitors</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C071664">GLN3 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C107270">MEP2 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C079378">RTG1 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C104438">RTG3 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D012097">Repressor Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029701">Saccharomyces cerevisiae Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D015534">Trans-Activators</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014157">Transcription Factors</NameOfSubstance></Chemical><Chemical><RegistryNumber>0RH81L854J</RegistryNumber><NameOfSubstance UI="D005973">Glutamine</NameOfSubstance></Chemical><Chemical><RegistryNumber>1982-67-8</RegistryNumber><NameOfSubstance UI="D008717">Methionine Sulfoximine</NameOfSubstance></Chemical><Chemical><RegistryNumber>3KX376GY7L</RegistryNumber><NameOfSubstance UI="D018698">Glutamic Acid</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 6.3.1.2</RegistryNumber><NameOfSubstance UI="D005974">Glutamate-Ammonia Ligase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D051778" MajorTopicYN="N">Basic Helix-Loop-Helix Leucine Zipper Transcription Factors</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002352" MajorTopicYN="N">Carrier Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D027682" MajorTopicYN="Y">Cation Transport Proteins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004268" MajorTopicYN="N">DNA-Binding Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004791" MajorTopicYN="N">Enzyme Inhibitors</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015870" MajorTopicYN="N">Gene Expression</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005974" MajorTopicYN="N">Glutamate-Ammonia Ligase</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018698" MajorTopicYN="N">Glutamic Acid</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005973" MajorTopicYN="N">Glutamine</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007424" MajorTopicYN="N">Intracellular Fluid</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008717" MajorTopicYN="N">Methionine Sulfoximine</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019869" MajorTopicYN="Y">Phosphatidylinositol 3-Kinases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017853" MajorTopicYN="N">Phosphotransferases (Alcohol Group Acceptor)</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012097" MajorTopicYN="Y">Repressor Proteins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000254" MajorTopicYN="N">growth & development</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029701" MajorTopicYN="Y">Saccharomyces cerevisiae Proteins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015398" MajorTopicYN="Y">Signal Transduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015534" MajorTopicYN="N">Trans-Activators</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014157" MajorTopicYN="Y">Transcription Factors</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2002</Year><Month>5</Month><Day>9</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2002</Year><Month>6</Month><Day>19</Day><Hour>10</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2002</Year><Month>5</Month><Day>9</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">11997479</ArticleId><ArticleId IdType="doi">10.1073/pnas.102687599</ArticleId><ArticleId IdType="pii">102687599</ArticleId><ArticleId IdType="pmc">PMC124480</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>J Biol Chem. 1998 Feb 13;273(7):3963-6</Citation><ArticleIdList><ArticleId IdType="pubmed">9461583</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Cell Biol. 1997 Mar;17(3):1110-7</Citation><ArticleIdList><ArticleId IdType="pubmed">9032238</ArticleId></ArticleIdList></Reference><Reference><Citation>J Bacteriol. 1998 Mar;180(5):1044-52</Citation><ArticleIdList><ArticleId IdType="pubmed">9495741</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1998 Jun 5;273(23):14484-94</Citation><ArticleIdList><ArticleId IdType="pubmed">9603962</ArticleId></ArticleIdList></Reference><Reference><Citation>EMBO J. 1998 Jul 1;17(13):3556-64</Citation><ArticleIdList><ArticleId IdType="pubmed">9649426</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Cell Biol. 1998 Aug;18(8):4463-70</Citation><ArticleIdList><ArticleId IdType="pubmed">9671456</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochem J. 1998 Aug 15;334 ( Pt 1):261-7</Citation><ArticleIdList><ArticleId IdType="pubmed">9693128</ArticleId></ArticleIdList></Reference><Reference><Citation>Yeast. 1998 Jul;14(10):953-61</Citation><ArticleIdList><ArticleId IdType="pubmed">9717241</ArticleId></ArticleIdList></Reference><Reference><Citation>EMBO J. 1998 Dec 1;17(23):6924-31</Citation><ArticleIdList><ArticleId IdType="pubmed">9843498</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Biol Cell. 1999 Apr;10(4):987-1000</Citation><ArticleIdList><ArticleId IdType="pubmed">10198052</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Cell Biol. 1999 Oct;19(10):6720-8</Citation><ArticleIdList><ArticleId IdType="pubmed">10490611</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Gen Genet. 1989 Jun;217(2-3):370-7</Citation><ArticleIdList><ArticleId IdType="pubmed">2570348</ArticleId></ArticleIdList></Reference><Reference><Citation>Nature. 1999 Dec 9;402(6762):689-92</Citation><ArticleIdList><ArticleId IdType="pubmed">10604478</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 1999 Dec 21;96(26):14866-70</Citation><ArticleIdList><ArticleId IdType="pubmed">10611304</ArticleId></ArticleIdList></Reference><Reference><Citation>Genes Dev. 1999 Dec 15;13(24):3271-9</Citation><ArticleIdList><ArticleId IdType="pubmed">10617575</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Biol Cell. 2000 Jun;11(6):2103-15</Citation><ArticleIdList><ArticleId IdType="pubmed">10848632</ArticleId></ArticleIdList></Reference><Reference><Citation>Cell. 2000 Oct 13;103(2):253-62</Citation><ArticleIdList><ArticleId IdType="pubmed">11057898</ArticleId></ArticleIdList></Reference><Reference><Citation>J Cell Biol. 2000 Nov 13;151(4):863-78</Citation><ArticleIdList><ArticleId IdType="pubmed">11076970</ArticleId></ArticleIdList></Reference><Reference><Citation>Curr Biol. 2000 Dec 14-28;10(24):1574-81</Citation><ArticleIdList><ArticleId IdType="pubmed">11137008</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 1969 Jun;8(6):2681-5</Citation><ArticleIdList><ArticleId IdType="pubmed">5799144</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1983 Jan 10;258(1):119-24</Citation><ArticleIdList><ArticleId IdType="pubmed">6129248</ArticleId></ArticleIdList></Reference><Reference><Citation>Cell. 1993 Jan 15;72(1):61-71</Citation><ArticleIdList><ArticleId IdType="pubmed">8422683</ArticleId></ArticleIdList></Reference><Reference><Citation>Cell. 1993 May 7;73(3):585-96</Citation><ArticleIdList><ArticleId IdType="pubmed">8387896</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 1995 Oct 10;92(21):9450-4</Citation><ArticleIdList><ArticleId IdType="pubmed">7568152</ArticleId></ArticleIdList></Reference><Reference><Citation>J Bacteriol. 1995 Dec;177(23):6910-8</Citation><ArticleIdList><ArticleId IdType="pubmed">7592485</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Biol Cell. 1996 Jan;7(1):25-42</Citation><ArticleIdList><ArticleId IdType="pubmed">8741837</ArticleId></ArticleIdList></Reference><Reference><Citation>Genes Dev. 1998 Feb 15;12(4):586-97</Citation><ArticleIdList><ArticleId IdType="pubmed">9472026</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>Suisse</li></country></list><tree><noCountry><name sortKey="Fowler, Brian" sort="Fowler, Brian" uniqKey="Fowler B" first="Brian" last="Fowler">Brian Fowler</name><name sortKey="Hall, Michael N" sort="Hall, Michael N" uniqKey="Hall M" first="Michael N" last="Hall">Michael N. Hall</name><name sortKey="Powers, Ted" sort="Powers, Ted" uniqKey="Powers T" first="Ted" last="Powers">Ted Powers</name></noCountry><country name="Suisse"><noRegion><name sortKey="Crespo, Jose L" sort="Crespo, Jose L" uniqKey="Crespo J" first="José L" last="Crespo">José L. Crespo</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Bois/explor/RapamycinFungusV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 001964 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 001964 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Bois
|area= RapamycinFungusV1
|flux= Main
|étape= Exploration
|type= RBID
|clé= pubmed:11997479
|texte= The TOR-controlled transcription activators GLN3, RTG1, and RTG3 are regulated in response to intracellular levels of glutamine.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:11997479" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a RapamycinFungusV1
| This area was generated with Dilib version V0.6.38. |  |