Alterations in the Ure2 αCap domain elicit different GATA factor responses to rapamycin treatment and nitrogen limitation.
Identifieur interne : 001076 ( Main/Exploration ); précédent : 001075; suivant : 001077Alterations in the Ure2 αCap domain elicit different GATA factor responses to rapamycin treatment and nitrogen limitation.
Auteurs : Andre Feller [Belgique] ; Isabelle Georis ; Jennifer J. Tate ; Terrance G. Cooper ; Evelyne DuboisSource :
- The Journal of biological chemistry [ 1083-351X ] ; 2013.
Descripteurs français
- KwdFr :
- Antifongiques (pharmacologie), Azote (déficit), Facteurs de transcription (génétique), Facteurs de transcription (métabolisme), Facteurs de transcription GATA (génétique), Facteurs de transcription GATA (métabolisme), Glutathione peroxidase (génétique), Glutathione peroxidase (métabolisme), Mutation (MeSH), Prions (génétique), Prions (métabolisme), Protéines de Saccharomyces cerevisiae (génétique), Protéines de Saccharomyces cerevisiae (métabolisme), Régulation de l'expression des gènes fongiques (effets des médicaments et des substances chimiques), Saccharomyces cerevisiae (génétique), Saccharomyces cerevisiae (métabolisme), Sirolimus (pharmacologie), Structure tertiaire des protéines (MeSH), Transduction du signal (effets des médicaments et des substances chimiques).
- MESH :
- déficit : Azote.
- effets des médicaments et des substances chimiques : Régulation de l'expression des gènes fongiques, Transduction du signal.
- génétique : Facteurs de transcription, Facteurs de transcription GATA, Glutathione peroxidase, Prions, Protéines de Saccharomyces cerevisiae, Saccharomyces cerevisiae.
- métabolisme : Facteurs de transcription, Facteurs de transcription GATA, Glutathione peroxidase, Prions, Protéines de Saccharomyces cerevisiae, Saccharomyces cerevisiae.
- pharmacologie : Antifongiques, Sirolimus.
- Mutation, Structure tertiaire des protéines.
English descriptors
- KwdEn :
- Antifungal Agents (pharmacology), GATA Transcription Factors (genetics), GATA Transcription Factors (metabolism), Gene Expression Regulation, Fungal (drug effects), Glutathione Peroxidase (genetics), Glutathione Peroxidase (metabolism), Mutation (MeSH), Nitrogen (deficiency), Prions (genetics), Prions (metabolism), Protein Structure, Tertiary (MeSH), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism), Signal Transduction (drug effects), Sirolimus (pharmacology), Transcription Factors (genetics), Transcription Factors (metabolism).
- MESH :
- chemical , deficiency : Nitrogen.
- chemical , genetics : GATA Transcription Factors, Glutathione Peroxidase, Prions, Saccharomyces cerevisiae Proteins, Transcription Factors.
- chemical , metabolism : GATA Transcription Factors, Glutathione Peroxidase, Prions, Saccharomyces cerevisiae Proteins, Transcription Factors.
- chemical , pharmacology : Antifungal Agents, Sirolimus.
- drug effects : Gene Expression Regulation, Fungal, Signal Transduction.
- genetics : Saccharomyces cerevisiae.
- metabolism : Saccharomyces cerevisiae.
- Mutation, Protein Structure, Tertiary.
Abstract
Ure2 is a phosphoprotein and central negative regulator of nitrogen-responsive Gln3/Gat1 localization and their ability to activate transcription. This negative regulation is achieved by the formation of Ure2-Gln3 and -Gat1 complexes that are thought to sequester these GATA factors in the cytoplasm of cells cultured in excess nitrogen. Ure2 itself is a dimer the monomer of which consists of two core domains and a flexible protruding αcap. Here, we show that alterations in this αcap abolish rapamycin-elicited nuclear Gln3 and, to a more limited extent, Gat1 localization. In contrast, these alterations have little demonstrable effect on the Gln3 and Gat1 responses to nitrogen limitation. Using two-dimensional PAGE we resolved eight rather than the two previously reported Ure2 isoforms and demonstrated Ure2 dephosphorylation to be stimulus-specific, occurring after rapamycin treatment but only minimally if at all in nitrogen-limited cells. Alteration of the αcap significantly diminished the response of Ure2 dephosphorylation to the TorC1 inhibitor, rapamycin. Furthermore, in contrast to Gln3, rapamycin-elicited Ure2 dephosphorylation occurred independently of Sit4 and Pph21/22 (PP2A) as well as Siw14, Ptc1, and Ppz1. Together, our data suggest that distinct regions of Ure2 are associated with the receipt and/or implementation of signals calling for cessation of GATA factor sequestration in the cytoplasm. This in turn is more consistent with the existence of distinct pathways for TorC1- and nitrogen limitation-dependent control than it is with these stimuli representing sequential steps in a single regulatory pathway.
DOI: 10.1074/jbc.M112.385054
PubMed: 23184930
PubMed Central: PMC3548494
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Alterations in the Ure2 αCap domain elicit different GATA factor responses to rapamycin treatment and nitrogen limitation.</title><author><name sortKey="Feller, Andre" sort="Feller, Andre" uniqKey="Feller A" first="Andre" last="Feller">Andre Feller</name><affiliation wicri:level="1"><nlm:affiliation>Institut de Recherches Microbiologiques J.-M. Wiame, Laboratoire de Microbiologie Université Libre de Bruxelles, B1070 Brussels, Belgium.</nlm:affiliation><country xml:lang="fr">Belgique</country><wicri:regionArea>Institut de Recherches Microbiologiques J.-M. Wiame, Laboratoire de Microbiologie Université Libre de Bruxelles, B1070 Brussels</wicri:regionArea><wicri:noRegion>B1070 Brussels</wicri:noRegion></affiliation></author><author><name sortKey="Georis, Isabelle" sort="Georis, Isabelle" uniqKey="Georis I" first="Isabelle" last="Georis">Isabelle Georis</name></author><author><name sortKey="Tate, Jennifer J" sort="Tate, Jennifer J" uniqKey="Tate J" first="Jennifer J" last="Tate">Jennifer J. Tate</name></author><author><name sortKey="Cooper, Terrance G" sort="Cooper, Terrance G" uniqKey="Cooper T" first="Terrance G" last="Cooper">Terrance G. Cooper</name></author><author><name sortKey="Dubois, Evelyne" sort="Dubois, Evelyne" uniqKey="Dubois E" first="Evelyne" last="Dubois">Evelyne Dubois</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2013">2013</date><idno type="RBID">pubmed:23184930</idno><idno type="pmid">23184930</idno><idno type="doi">10.1074/jbc.M112.385054</idno><idno type="pmc">PMC3548494</idno><idno type="wicri:Area/Main/Corpus">001080</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">001080</idno><idno type="wicri:Area/Main/Curation">001080</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">001080</idno><idno type="wicri:Area/Main/Exploration">001080</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Alterations in the Ure2 αCap domain elicit different GATA factor responses to rapamycin treatment and nitrogen limitation.</title><author><name sortKey="Feller, Andre" sort="Feller, Andre" uniqKey="Feller A" first="Andre" last="Feller">Andre Feller</name><affiliation wicri:level="1"><nlm:affiliation>Institut de Recherches Microbiologiques J.-M. Wiame, Laboratoire de Microbiologie Université Libre de Bruxelles, B1070 Brussels, Belgium.</nlm:affiliation><country xml:lang="fr">Belgique</country><wicri:regionArea>Institut de Recherches Microbiologiques J.-M. Wiame, Laboratoire de Microbiologie Université Libre de Bruxelles, B1070 Brussels</wicri:regionArea><wicri:noRegion>B1070 Brussels</wicri:noRegion></affiliation></author><author><name sortKey="Georis, Isabelle" sort="Georis, Isabelle" uniqKey="Georis I" first="Isabelle" last="Georis">Isabelle Georis</name></author><author><name sortKey="Tate, Jennifer J" sort="Tate, Jennifer J" uniqKey="Tate J" first="Jennifer J" last="Tate">Jennifer J. Tate</name></author><author><name sortKey="Cooper, Terrance G" sort="Cooper, Terrance G" uniqKey="Cooper T" first="Terrance G" last="Cooper">Terrance G. Cooper</name></author><author><name sortKey="Dubois, Evelyne" sort="Dubois, Evelyne" uniqKey="Dubois E" first="Evelyne" last="Dubois">Evelyne Dubois</name></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="eISSN">1083-351X</idno><imprint><date when="2013" type="published">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Antifungal Agents (pharmacology)</term><term>GATA Transcription Factors (genetics)</term><term>GATA Transcription Factors (metabolism)</term><term>Gene Expression Regulation, Fungal (drug effects)</term><term>Glutathione Peroxidase (genetics)</term><term>Glutathione Peroxidase (metabolism)</term><term>Mutation (MeSH)</term><term>Nitrogen (deficiency)</term><term>Prions (genetics)</term><term>Prions (metabolism)</term><term>Protein Structure, Tertiary (MeSH)</term><term>Saccharomyces cerevisiae (genetics)</term><term>Saccharomyces cerevisiae (metabolism)</term><term>Saccharomyces cerevisiae Proteins (genetics)</term><term>Saccharomyces cerevisiae Proteins (metabolism)</term><term>Signal Transduction (drug effects)</term><term>Sirolimus (pharmacology)</term><term>Transcription Factors (genetics)</term><term>Transcription Factors (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Antifongiques (pharmacologie)</term><term>Azote (déficit)</term><term>Facteurs de transcription (génétique)</term><term>Facteurs de transcription (métabolisme)</term><term>Facteurs de transcription GATA (génétique)</term><term>Facteurs de transcription GATA (métabolisme)</term><term>Glutathione peroxidase (génétique)</term><term>Glutathione peroxidase (métabolisme)</term><term>Mutation (MeSH)</term><term>Prions (génétique)</term><term>Prions (métabolisme)</term><term>Protéines de Saccharomyces cerevisiae (génétique)</term><term>Protéines de Saccharomyces cerevisiae (métabolisme)</term><term>Régulation de l'expression des gènes fongiques (effets des médicaments et des substances chimiques)</term><term>Saccharomyces cerevisiae (génétique)</term><term>Saccharomyces cerevisiae (métabolisme)</term><term>Sirolimus (pharmacologie)</term><term>Structure tertiaire des protéines (MeSH)</term><term>Transduction du signal (effets des médicaments et des substances chimiques)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="deficiency" xml:lang="en"><term>Nitrogen</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>GATA Transcription Factors</term><term>Glutathione Peroxidase</term><term>Prions</term><term>Saccharomyces cerevisiae Proteins</term><term>Transcription Factors</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>GATA Transcription Factors</term><term>Glutathione Peroxidase</term><term>Prions</term><term>Saccharomyces cerevisiae Proteins</term><term>Transcription Factors</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Antifungal Agents</term><term>Sirolimus</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Gene Expression Regulation, Fungal</term><term>Signal Transduction</term></keywords><keywords scheme="MESH" qualifier="déficit" xml:lang="fr"><term>Azote</term></keywords><keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Régulation de l'expression des gènes fongiques</term><term>Transduction du signal</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Facteurs de transcription</term><term>Facteurs de transcription GATA</term><term>Glutathione peroxidase</term><term>Prions</term><term>Protéines de Saccharomyces cerevisiae</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Facteurs de transcription</term><term>Facteurs de transcription GATA</term><term>Glutathione peroxidase</term><term>Prions</term><term>Protéines de Saccharomyces cerevisiae</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Antifongiques</term><term>Sirolimus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Mutation</term><term>Protein Structure, Tertiary</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Mutation</term><term>Structure tertiaire des protéines</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Ure2 is a phosphoprotein and central negative regulator of nitrogen-responsive Gln3/Gat1 localization and their ability to activate transcription. This negative regulation is achieved by the formation of Ure2-Gln3 and -Gat1 complexes that are thought to sequester these GATA factors in the cytoplasm of cells cultured in excess nitrogen. Ure2 itself is a dimer the monomer of which consists of two core domains and a flexible protruding αcap. Here, we show that alterations in this αcap abolish rapamycin-elicited nuclear Gln3 and, to a more limited extent, Gat1 localization. In contrast, these alterations have little demonstrable effect on the Gln3 and Gat1 responses to nitrogen limitation. Using two-dimensional PAGE we resolved eight rather than the two previously reported Ure2 isoforms and demonstrated Ure2 dephosphorylation to be stimulus-specific, occurring after rapamycin treatment but only minimally if at all in nitrogen-limited cells. Alteration of the αcap significantly diminished the response of Ure2 dephosphorylation to the TorC1 inhibitor, rapamycin. Furthermore, in contrast to Gln3, rapamycin-elicited Ure2 dephosphorylation occurred independently of Sit4 and Pph21/22 (PP2A) as well as Siw14, Ptc1, and Ppz1. Together, our data suggest that distinct regions of Ure2 are associated with the receipt and/or implementation of signals calling for cessation of GATA factor sequestration in the cytoplasm. This in turn is more consistent with the existence of distinct pathways for TorC1- and nitrogen limitation-dependent control than it is with these stimuli representing sequential steps in a single regulatory pathway.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">23184930</PMID><DateCompleted><Year>2013</Year><Month>03</Month><Day>26</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1083-351X</ISSN><JournalIssue CitedMedium="Internet"><Volume>288</Volume><Issue>3</Issue><PubDate><Year>2013</Year><Month>Jan</Month><Day>18</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Alterations in the Ure2 αCap domain elicit different GATA factor responses to rapamycin treatment and nitrogen limitation.</ArticleTitle><Pagination><MedlinePgn>1841-55</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1074/jbc.M112.385054</ELocationID><Abstract><AbstractText>Ure2 is a phosphoprotein and central negative regulator of nitrogen-responsive Gln3/Gat1 localization and their ability to activate transcription. This negative regulation is achieved by the formation of Ure2-Gln3 and -Gat1 complexes that are thought to sequester these GATA factors in the cytoplasm of cells cultured in excess nitrogen. Ure2 itself is a dimer the monomer of which consists of two core domains and a flexible protruding αcap. Here, we show that alterations in this αcap abolish rapamycin-elicited nuclear Gln3 and, to a more limited extent, Gat1 localization. In contrast, these alterations have little demonstrable effect on the Gln3 and Gat1 responses to nitrogen limitation. Using two-dimensional PAGE we resolved eight rather than the two previously reported Ure2 isoforms and demonstrated Ure2 dephosphorylation to be stimulus-specific, occurring after rapamycin treatment but only minimally if at all in nitrogen-limited cells. Alteration of the αcap significantly diminished the response of Ure2 dephosphorylation to the TorC1 inhibitor, rapamycin. Furthermore, in contrast to Gln3, rapamycin-elicited Ure2 dephosphorylation occurred independently of Sit4 and Pph21/22 (PP2A) as well as Siw14, Ptc1, and Ppz1. Together, our data suggest that distinct regions of Ure2 are associated with the receipt and/or implementation of signals calling for cessation of GATA factor sequestration in the cytoplasm. This in turn is more consistent with the existence of distinct pathways for TorC1- and nitrogen limitation-dependent control than it is with these stimuli representing sequential steps in a single regulatory pathway.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Feller</LastName><ForeName>Andre</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Institut de Recherches Microbiologiques J.-M. Wiame, Laboratoire de Microbiologie Université Libre de Bruxelles, B1070 Brussels, Belgium.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Georis</LastName><ForeName>Isabelle</ForeName><Initials>I</Initials></Author><Author ValidYN="Y"><LastName>Tate</LastName><ForeName>Jennifer J</ForeName><Initials>JJ</Initials></Author><Author ValidYN="Y"><LastName>Cooper</LastName><ForeName>Terrance G</ForeName><Initials>TG</Initials></Author><Author ValidYN="Y"><LastName>Dubois</LastName><ForeName>Evelyne</ForeName><Initials>E</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01 GM035642</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>GM-35642-23A1</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2012</Year><Month>11</Month><Day>26</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Biol Chem</MedlineTA><NlmUniqueID>2985121R</NlmUniqueID><ISSNLinking>0021-9258</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000935">Antifungal Agents</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C096100">GAT1 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D050980">GATA Transcription Factors</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C071664">GLN3 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011328">Prions</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029701">Saccharomyces cerevisiae Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C561842">TORC1 protein complex, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014157">Transcription Factors</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.9</RegistryNumber><NameOfSubstance UI="D005979">Glutathione Peroxidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.9</RegistryNumber><NameOfSubstance UI="C067020">URE2 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>N762921K75</RegistryNumber><NameOfSubstance UI="D009584">Nitrogen</NameOfSubstance></Chemical><Chemical><RegistryNumber>W36ZG6FT64</RegistryNumber><NameOfSubstance UI="D020123">Sirolimus</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000935" MajorTopicYN="N">Antifungal Agents</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D050980" MajorTopicYN="N">GATA Transcription Factors</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015966" MajorTopicYN="N">Gene Expression Regulation, Fungal</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005979" MajorTopicYN="N">Glutathione Peroxidase</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009584" MajorTopicYN="N">Nitrogen</DescriptorName><QualifierName UI="Q000172" MajorTopicYN="Y">deficiency</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011328" MajorTopicYN="N">Prions</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017434" MajorTopicYN="N">Protein Structure, Tertiary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029701" MajorTopicYN="N">Saccharomyces cerevisiae Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015398" MajorTopicYN="N">Signal Transduction</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020123" MajorTopicYN="N">Sirolimus</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014157" MajorTopicYN="N">Transcription Factors</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2012</Year><Month>11</Month><Day>28</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2012</Year><Month>11</Month><Day>28</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2013</Year><Month>3</Month><Day>27</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">23184930</ArticleId><ArticleId IdType="pii">M112.385054</ArticleId><ArticleId IdType="doi">10.1074/jbc.M112.385054</ArticleId><ArticleId IdType="pmc">PMC3548494</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>Mol Biotechnol. 1999 Aug;12(1):35-73</Citation><ArticleIdList><ArticleId IdType="pubmed">10554772</ArticleId></ArticleIdList></Reference><Reference><Citation>Gene. 2002 May 15;290(1-2):1-18</Citation><ArticleIdList><ArticleId IdType="pubmed">12062797</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>J Biol Chem. 2000 May 12;275(19):14408-14</Citation><ArticleIdList><ArticleId IdType="pubmed">10799523</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2000 Nov 17;275(46):35727-33</Citation><ArticleIdList><ArticleId IdType="pubmed">10940301</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>Proc Natl Acad Sci U S A. 2001 Feb 13;98(4):1459-64</Citation><ArticleIdList><ArticleId IdType="pubmed">11171973</ArticleId></ArticleIdList></Reference><Reference><Citation>Structure. 2001 Jan 10;9(1):39-46</Citation><ArticleIdList><ArticleId IdType="pubmed">11342133</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2001 Aug 24;276(34):32136-44</Citation><ArticleIdList><ArticleId IdType="pubmed">11408486</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochemistry. 2001 Nov 13;40(45):13564-73</Citation><ArticleIdList><ArticleId IdType="pubmed">11695904</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2002 Oct 4;277(40):37559-66</Citation><ArticleIdList><ArticleId IdType="pubmed">12140287</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2003 May 9;278(19):16878-86</Citation><ArticleIdList><ArticleId IdType="pubmed">12624103</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Cell. 2003 Jun;11(6):1467-78</Citation><ArticleIdList><ArticleId IdType="pubmed">12820961</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Biol Cell. 2003 Nov;14(11):4342-51</Citation><ArticleIdList><ArticleId IdType="pubmed">14551259</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2004 Mar 12;279(11):10270-8</Citation><ArticleIdList><ArticleId IdType="pubmed">14679193</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2004 Apr 30;279(18):19294-301</Citation><ArticleIdList><ArticleId IdType="pubmed">14970238</ArticleId></ArticleIdList></Reference><Reference><Citation>J Bacteriol. 1971 May;106(2):519-22</Citation><ArticleIdList><ArticleId IdType="pubmed">5573734</ArticleId></ArticleIdList></Reference><Reference><Citation>J Bacteriol. 1972 Jan;109(1):203-8</Citation><ArticleIdList><ArticleId IdType="pubmed">4550662</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochem Biophys Res Commun. 1973 Jul 17;53(2):367-72</Citation><ArticleIdList><ArticleId IdType="pubmed">4146147</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Gen Genet. 1974;128(1):73-85</Citation><ArticleIdList><ArticleId IdType="pubmed">4150855</ArticleId></ArticleIdList></Reference><Reference><Citation>Yeast. 1991 Aug-Sep;7(6):609-15</Citation><ArticleIdList><ArticleId IdType="pubmed">1767589</ArticleId></ArticleIdList></Reference><Reference><Citation>Science. 1995 Oct 6;270(5233):93-5</Citation><ArticleIdList><ArticleId IdType="pubmed">7569955</ArticleId></ArticleIdList></Reference><Reference><Citation>J Bacteriol. 1996 Aug;178(15):4734-6</Citation><ArticleIdList><ArticleId IdType="pubmed">8755910</ArticleId></ArticleIdList></Reference><Reference><Citation>Yeast. 1996 Mar 15;12(3):259-65</Citation><ArticleIdList><ArticleId IdType="pubmed">8904338</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 1997 Nov 11;94(23):12503-8</Citation><ArticleIdList><ArticleId IdType="pubmed">9356479</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Biol Cell. 1997 Dec;8(12):2677-91</Citation><ArticleIdList><ArticleId IdType="pubmed">9398684</ArticleId></ArticleIdList></Reference><Reference><Citation>Yeast. 1998 Jul;14(10):953-61</Citation><ArticleIdList><ArticleId IdType="pubmed">9717241</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1999 Jan 8;274(2):555-8</Citation><ArticleIdList><ArticleId IdType="pubmed">9872986</ArticleId></ArticleIdList></Reference><Reference><Citation>EMBO J. 1999 May 17;18(10):2782-92</Citation><ArticleIdList><ArticleId IdType="pubmed">10329624</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Cell Biol. 1999 Jun;19(6):4516-24</Citation><ArticleIdList><ArticleId IdType="pubmed">10330190</ArticleId></ArticleIdList></Reference><Reference><Citation>Science. 1999 Aug 6;285(5429):901-6</Citation><ArticleIdList><ArticleId IdType="pubmed">10436161</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2005 Jul 22;280(29):27195-204</Citation><ArticleIdList><ArticleId IdType="pubmed">15911613</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Gen Genet. 1975;136(4):327-35</Citation><ArticleIdList><ArticleId IdType="pubmed">16095000</ArticleId></ArticleIdList></Reference><Reference><Citation>Microbiol Mol Biol Rev. 2006 Jun;70(2):440-9</Citation><ArticleIdList><ArticleId IdType="pubmed">16760309</ArticleId></ArticleIdList></Reference><Reference><Citation>EMBO J. 2006 Aug 9;25(15):3546-55</Citation><ArticleIdList><ArticleId IdType="pubmed">16874307</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2006 Sep 22;281(38):28460-9</Citation><ArticleIdList><ArticleId IdType="pubmed">16864577</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2006 Dec 8;281(49):37980-92</Citation><ArticleIdList><ArticleId IdType="pubmed">17015442</ArticleId></ArticleIdList></Reference><Reference><Citation>Bioinformatics. 2007 Apr 1;23(7):895-7</Citation><ArticleIdList><ArticleId IdType="pubmed">17282998</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2007 Jun 22;282(25):18467-80</Citation><ArticleIdList><ArticleId IdType="pubmed">17439949</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Cell Biol. 2008 Jan;28(2):551-63</Citation><ArticleIdList><ArticleId IdType="pubmed">17984223</ArticleId></ArticleIdList></Reference><Reference><Citation>Gene. 2008 Feb 15;409(1-2):34-43</Citation><ArticleIdList><ArticleId IdType="pubmed">18166280</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2008 Apr 4;283(14):8919-29</Citation><ArticleIdList><ArticleId IdType="pubmed">18245087</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 2008 May 20;105(20):7194-9</Citation><ArticleIdList><ArticleId IdType="pubmed">18443284</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2009 Jan 23;284(4):2522-34</Citation><ArticleIdList><ArticleId IdType="pubmed">19015262</ArticleId></ArticleIdList></Reference><Reference><Citation>Genetics. 2009 Mar;181(3):861-74</Citation><ArticleIdList><ArticleId IdType="pubmed">19104072</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Cell Biol. 2009 May;29(10):2876-88</Citation><ArticleIdList><ArticleId IdType="pubmed">19273591</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biosci Bioeng. 2010 May;109(5):433-41</Citation><ArticleIdList><ArticleId IdType="pubmed">20347764</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2010 Jun 4;285(23):17880-95</Citation><ArticleIdList><ArticleId IdType="pubmed">20378536</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Cell Biol. 2011 Jan;31(1):92-104</Citation><ArticleIdList><ArticleId IdType="pubmed">20974806</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biosci Bioeng. 2011 Mar;111(3):249-54</Citation><ArticleIdList><ArticleId IdType="pubmed">21237705</ArticleId></ArticleIdList></Reference><Reference><Citation>Genetics. 2011 Dec;189(4):1177-201</Citation><ArticleIdList><ArticleId IdType="pubmed">22174183</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2011 Dec 30;286(52):44897-912</Citation><ArticleIdList><ArticleId IdType="pubmed">22039046</ArticleId></ArticleIdList></Reference><Reference><Citation>Genetics. 2012 Mar;190(3):885-929</Citation><ArticleIdList><ArticleId IdType="pubmed">22419079</ArticleId></ArticleIdList></Reference><Reference><Citation>Genetics. 2012 Sep;192(1):73-105</Citation><ArticleIdList><ArticleId IdType="pubmed">22964838</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Cell. 2001 Nov;8(5):1017-26</Citation><ArticleIdList><ArticleId IdType="pubmed">11741537</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 2002 May 14;99(10):6784-9</Citation><ArticleIdList><ArticleId IdType="pubmed">11997479</ArticleId></ArticleIdList></Reference><Reference><Citation>Nature. 1999 Dec 9;402(6762):689-92</Citation><ArticleIdList><ArticleId IdType="pubmed">10604478</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>Belgique</li></country></list><tree><noCountry><name sortKey="Cooper, Terrance G" sort="Cooper, Terrance G" uniqKey="Cooper T" first="Terrance G" last="Cooper">Terrance G. Cooper</name><name sortKey="Dubois, Evelyne" sort="Dubois, Evelyne" uniqKey="Dubois E" first="Evelyne" last="Dubois">Evelyne Dubois</name><name sortKey="Georis, Isabelle" sort="Georis, Isabelle" uniqKey="Georis I" first="Isabelle" last="Georis">Isabelle Georis</name><name sortKey="Tate, Jennifer J" sort="Tate, Jennifer J" uniqKey="Tate J" first="Jennifer J" last="Tate">Jennifer J. Tate</name></noCountry><country name="Belgique"><noRegion><name sortKey="Feller, Andre" sort="Feller, Andre" uniqKey="Feller A" first="Andre" last="Feller">Andre Feller</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 001076 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 001076 | 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:23184930
|texte= Alterations in the Ure2 αCap domain elicit different GATA factor responses to rapamycin treatment and nitrogen limitation.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:23184930" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a RapamycinFungusV1
| This area was generated with Dilib version V0.6.38. |  |