RapamycinFungusV1, Main, Exploration, bibRecord, 001796

Carbon catabolite repression regulates amino acid permeases in Saccharomyces cerevisiae via the TOR signaling pathway.

Identifieur interne : 001796 ( Main/Exploration ); précédent : 001795; suivant : 001797

Carbon catabolite repression regulates amino acid permeases in Saccharomyces cerevisiae via the TOR signaling pathway.

Auteurs : George J. Peter [Royaume-Uni] ; Louis Düring ; Aamir Ahmed

Source :

The Journal of biological chemistry [ 0021-9258 ] ; 2006.

RBID : pubmed:16407266

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Transport Systems (metabolism), Amino Acids (chemistry), Amino Acids (metabolism), Culture Media (chemistry), DNA-Binding Proteins (metabolism), Fungal Proteins (metabolism), Protein-Serine-Threonine Kinases (MeSH), Recombinant Fusion Proteins (genetics), Recombinant Fusion Proteins (metabolism), Repressor Proteins (metabolism), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism), Signal Transduction (physiology).
MESH :
- chemical , chemistry : Amino Acids, Culture Media.
- chemical , genetics : Recombinant Fusion Proteins, Saccharomyces cerevisiae Proteins.
- chemical , metabolism : Amino Acid Transport Systems, Amino Acids, DNA-Binding Proteins, Fungal Proteins, Recombinant Fusion Proteins, Repressor Proteins, Saccharomyces cerevisiae Proteins.
- chemical : Protein-Serine-Threonine Kinases.
- genetics : Saccharomyces cerevisiae.
- metabolism : Saccharomyces cerevisiae.
- physiology : Signal Transduction.

Abstract

We have identified carbon catabolite repression (CCR) as a regulator of amino acid permeases in Saccharomyces cerevisiae, elucidated the permeases regulated by CCR, and identified the mechanisms involved in amino acid permease regulation by CCR. Transport of l-arginine and l-leucine was increased by approximately 10-25-fold in yeast grown in carbon sources alternate to glucose, indicating regulation by CCR. In wild type yeast the uptake (pmol/10(6) cells/h), in glucose versus galactose medium, of l-[(14)C]arginine was (0.24 +/- 0.04 versus 6.11 +/- 0.42) and l-[(14)C]leucine was (0.30 +/- 0.02 versus 3.60 +/- 0.50). The increase in amino acid uptake was maintained when galactose was replaced with glycerol. Deletion of gap1Delta and agp1Delta from the wild type strain did not alter CCR induced increase in l-leucine uptake; however, deletion of further amino acid permeases reduced the increase in l-leucine uptake in the following manner: 36% (gnp1Delta), 62% (bap2Delta), 83% (Delta(bap2-tat1)). Direct immunofluorescence showed large increases in the expression of Gnp1 and Bap2 proteins when grown in galactose compared with glucose medium. By extending the functional genomic approach to include major nutritional transducers of CCR in yeast, we concluded that SNF/MIG, GCN, or PSK pathways were not involved in the regulation of amino acid permeases by CCR. Strikingly, the deletion of TOR1, which regulates cellular response to changes in nitrogen availability, from the wild type strain abolished the CCR-induced amino acid uptake. Our results provide novel insights into the regulation of yeast amino acid permeases and signaling mechanisms involved in this regulation.

DOI: 10.1074/jbc.M513842200
PubMed: 16407266

Affiliations:

Links toward previous steps (curation, corpus...)

to stream Main, to step Corpus: 001802
to stream Main, to step Curation: 001802

Le document en format XML

<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Carbon catabolite repression regulates amino acid permeases in Saccharomyces cerevisiae via the TOR signaling pathway.</title>
<author><name sortKey="Peter, George J" sort="Peter, George J" uniqKey="Peter G" first="George J" last="Peter">George J. Peter</name>
<affiliation wicri:level="4"><nlm:affiliation>Institute of Urology and Nephrology, University College London, 67 Riding House Street, London W1W 7EY, United Kingdom.</nlm:affiliation>
<country xml:lang="fr">Royaume-Uni</country>
<wicri:regionArea>Institute of Urology and Nephrology, University College London, 67 Riding House Street, London W1W 7EY</wicri:regionArea>
<orgName type="university">University College de Londres</orgName>
<placeName><settlement type="city">Londres</settlement>
<region type="country">Angleterre</region>
<region type="région" nuts="1">Grand Londres</region>
</placeName>
</affiliation>
</author>
<author><name sortKey="During, Louis" sort="During, Louis" uniqKey="During L" first="Louis" last="Düring">Louis Düring</name>
</author>
<author><name sortKey="Ahmed, Aamir" sort="Ahmed, Aamir" uniqKey="Ahmed A" first="Aamir" last="Ahmed">Aamir Ahmed</name>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PubMed</idno>
<date when="2006">2006</date>
<idno type="RBID">pubmed:16407266</idno>
<idno type="pmid">16407266</idno>
<idno type="doi">10.1074/jbc.M513842200</idno>
<idno type="wicri:Area/Main/Corpus">001802</idno>
<idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">001802</idno>
<idno type="wicri:Area/Main/Curation">001802</idno>
<idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">001802</idno>
<idno type="wicri:Area/Main/Exploration">001802</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en">Carbon catabolite repression regulates amino acid permeases in Saccharomyces cerevisiae via the TOR signaling pathway.</title>
<author><name sortKey="Peter, George J" sort="Peter, George J" uniqKey="Peter G" first="George J" last="Peter">George J. Peter</name>
<affiliation wicri:level="4"><nlm:affiliation>Institute of Urology and Nephrology, University College London, 67 Riding House Street, London W1W 7EY, United Kingdom.</nlm:affiliation>
<country xml:lang="fr">Royaume-Uni</country>
<wicri:regionArea>Institute of Urology and Nephrology, University College London, 67 Riding House Street, London W1W 7EY</wicri:regionArea>
<orgName type="university">University College de Londres</orgName>
<placeName><settlement type="city">Londres</settlement>
<region type="country">Angleterre</region>
<region type="région" nuts="1">Grand Londres</region>
</placeName>
</affiliation>
</author>
<author><name sortKey="During, Louis" sort="During, Louis" uniqKey="During L" first="Louis" last="Düring">Louis Düring</name>
</author>
<author><name sortKey="Ahmed, Aamir" sort="Ahmed, Aamir" uniqKey="Ahmed A" first="Aamir" last="Ahmed">Aamir Ahmed</name>
</author>
</analytic>
<series><title level="j">The Journal of biological chemistry</title>
<idno type="ISSN">0021-9258</idno>
<imprint><date when="2006" type="published">2006</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Transport Systems (metabolism)</term>
<term>Amino Acids (chemistry)</term>
<term>Amino Acids (metabolism)</term>
<term>Culture Media (chemistry)</term>
<term>DNA-Binding Proteins (metabolism)</term>
<term>Fungal Proteins (metabolism)</term>
<term>Protein-Serine-Threonine Kinases (MeSH)</term>
<term>Recombinant Fusion Proteins (genetics)</term>
<term>Recombinant Fusion Proteins (metabolism)</term>
<term>Repressor Proteins (metabolism)</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 (physiology)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Acides aminés (composition chimique)</term>
<term>Acides aminés (métabolisme)</term>
<term>Milieux de culture (composition chimique)</term>
<term>Protein-Serine-Threonine Kinases (MeSH)</term>
<term>Protéines de Saccharomyces cerevisiae (génétique)</term>
<term>Protéines de Saccharomyces cerevisiae (métabolisme)</term>
<term>Protéines de fusion recombinantes (génétique)</term>
<term>Protéines de fusion recombinantes (métabolisme)</term>
<term>Protéines de liaison à l'ADN (métabolisme)</term>
<term>Protéines de répression (métabolisme)</term>
<term>Protéines fongiques (métabolisme)</term>
<term>Saccharomyces cerevisiae (génétique)</term>
<term>Saccharomyces cerevisiae (métabolisme)</term>
<term>Systèmes de transport d'acides aminés (métabolisme)</term>
<term>Transduction du signal (physiologie)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Amino Acids</term>
<term>Culture Media</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Recombinant Fusion Proteins</term>
<term>Saccharomyces cerevisiae Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Amino Acid Transport Systems</term>
<term>Amino Acids</term>
<term>DNA-Binding Proteins</term>
<term>Fungal Proteins</term>
<term>Recombinant Fusion Proteins</term>
<term>Repressor Proteins</term>
<term>Saccharomyces cerevisiae Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" xml:lang="en"><term>Protein-Serine-Threonine Kinases</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Acides aminés</term>
<term>Milieux de culture</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Protéines de Saccharomyces cerevisiae</term>
<term>Protéines de fusion recombinantes</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>Acides aminés</term>
<term>Protéines de Saccharomyces cerevisiae</term>
<term>Protéines de fusion recombinantes</term>
<term>Protéines de liaison à l'ADN</term>
<term>Protéines de répression</term>
<term>Protéines fongiques</term>
<term>Saccharomyces cerevisiae</term>
<term>Systèmes de transport d'acides aminés</term>
</keywords>
<keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Transduction du signal</term>
</keywords>
<keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Signal Transduction</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Protein-Serine-Threonine Kinases</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">We have identified carbon catabolite repression (CCR) as a regulator of amino acid permeases in Saccharomyces cerevisiae, elucidated the permeases regulated by CCR, and identified the mechanisms involved in amino acid permease regulation by CCR. Transport of l-arginine and l-leucine was increased by approximately 10-25-fold in yeast grown in carbon sources alternate to glucose, indicating regulation by CCR. In wild type yeast the uptake (pmol/10(6) cells/h), in glucose versus galactose medium, of l-[(14)C]arginine was (0.24 +/- 0.04 versus 6.11 +/- 0.42) and l-[(14)C]leucine was (0.30 +/- 0.02 versus 3.60 +/- 0.50). The increase in amino acid uptake was maintained when galactose was replaced with glycerol. Deletion of gap1Delta and agp1Delta from the wild type strain did not alter CCR induced increase in l-leucine uptake; however, deletion of further amino acid permeases reduced the increase in l-leucine uptake in the following manner: 36% (gnp1Delta), 62% (bap2Delta), 83% (Delta(bap2-tat1)). Direct immunofluorescence showed large increases in the expression of Gnp1 and Bap2 proteins when grown in galactose compared with glucose medium. By extending the functional genomic approach to include major nutritional transducers of CCR in yeast, we concluded that SNF/MIG, GCN, or PSK pathways were not involved in the regulation of amino acid permeases by CCR. Strikingly, the deletion of TOR1, which regulates cellular response to changes in nitrogen availability, from the wild type strain abolished the CCR-induced amino acid uptake. Our results provide novel insights into the regulation of yeast amino acid permeases and signaling mechanisms involved in this regulation.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16407266</PMID>
<DateCompleted><Year>2006</Year>
<Month>05</Month>
<Day>23</Day>
</DateCompleted>
<DateRevised><Year>2008</Year>
<Month>11</Month>
<Day>21</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0021-9258</ISSN>
<JournalIssue CitedMedium="Print"><Volume>281</Volume>
<Issue>9</Issue>
<PubDate><Year>2006</Year>
<Month>Mar</Month>
<Day>03</Day>
</PubDate>
</JournalIssue>
<Title>The Journal of biological chemistry</Title>
<ISOAbbreviation>J Biol Chem</ISOAbbreviation>
</Journal>
<ArticleTitle>Carbon catabolite repression regulates amino acid permeases in Saccharomyces cerevisiae via the TOR signaling pathway.</ArticleTitle>
<Pagination><MedlinePgn>5546-52</MedlinePgn>
</Pagination>
<Abstract><AbstractText>We have identified carbon catabolite repression (CCR) as a regulator of amino acid permeases in Saccharomyces cerevisiae, elucidated the permeases regulated by CCR, and identified the mechanisms involved in amino acid permease regulation by CCR. Transport of l-arginine and l-leucine was increased by approximately 10-25-fold in yeast grown in carbon sources alternate to glucose, indicating regulation by CCR. In wild type yeast the uptake (pmol/10(6) cells/h), in glucose versus galactose medium, of l-[(14)C]arginine was (0.24 +/- 0.04 versus 6.11 +/- 0.42) and l-[(14)C]leucine was (0.30 +/- 0.02 versus 3.60 +/- 0.50). The increase in amino acid uptake was maintained when galactose was replaced with glycerol. Deletion of gap1Delta and agp1Delta from the wild type strain did not alter CCR induced increase in l-leucine uptake; however, deletion of further amino acid permeases reduced the increase in l-leucine uptake in the following manner: 36% (gnp1Delta), 62% (bap2Delta), 83% (Delta(bap2-tat1)). Direct immunofluorescence showed large increases in the expression of Gnp1 and Bap2 proteins when grown in galactose compared with glucose medium. By extending the functional genomic approach to include major nutritional transducers of CCR in yeast, we concluded that SNF/MIG, GCN, or PSK pathways were not involved in the regulation of amino acid permeases by CCR. Strikingly, the deletion of TOR1, which regulates cellular response to changes in nitrogen availability, from the wild type strain abolished the CCR-induced amino acid uptake. Our results provide novel insights into the regulation of yeast amino acid permeases and signaling mechanisms involved in this regulation.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Peter</LastName>
<ForeName>George J</ForeName>
<Initials>GJ</Initials>
<AffiliationInfo><Affiliation>Institute of Urology and Nephrology, University College London, 67 Riding House Street, London W1W 7EY, United Kingdom.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Düring</LastName>
<ForeName>Louis</ForeName>
<Initials>L</Initials>
</Author>
<Author ValidYN="Y"><LastName>Ahmed</LastName>
<ForeName>Aamir</ForeName>
<Initials>A</Initials>
</Author>
</AuthorList>
<Language>eng</Language>
<GrantList CompleteYN="Y"><Grant><Agency>Wellcome Trust</Agency>
<Country>United Kingdom</Country>
</Grant>
</GrantList>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2006</Year>
<Month>01</Month>
<Day>04</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="D026905">Amino Acid Transport Systems</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D000596">Amino Acids</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D003470">Culture Media</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D004268">DNA-Binding Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D011993">Recombinant Fusion Proteins</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>EC 2.7.11.1</RegistryNumber>
<NameOfSubstance UI="D017346">Protein-Serine-Threonine Kinases</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber>
<NameOfSubstance UI="C500749">target of rapamycin protein, S cerevisiae</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D026905" MajorTopicYN="N">Amino Acid Transport Systems</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000596" MajorTopicYN="N">Amino Acids</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D003470" MajorTopicYN="N">Culture Media</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D004268" MajorTopicYN="N">DNA-Binding Proteins</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D017346" MajorTopicYN="N">Protein-Serine-Threonine Kinases</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011993" MajorTopicYN="N">Recombinant Fusion Proteins</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D012097" MajorTopicYN="N">Repressor Proteins</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D029701" MajorTopicYN="N">Saccharomyces cerevisiae Proteins</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<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>
</MeshHeadingList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2006</Year>
<Month>1</Month>
<Day>13</Day>
<Hour>9</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>2006</Year>
<Month>5</Month>
<Day>24</Day>
<Hour>9</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez"><Year>2006</Year>
<Month>1</Month>
<Day>13</Day>
<Hour>9</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList><ArticleId IdType="pubmed">16407266</ArticleId>
<ArticleId IdType="pii">M513842200</ArticleId>
<ArticleId IdType="doi">10.1074/jbc.M513842200</ArticleId>
</ArticleIdList>
</PubmedData>
</pubmed>
<affiliations><list><country><li>Royaume-Uni</li>
</country>
<region><li>Angleterre</li>
<li>Grand Londres</li>
</region>
<settlement><li>Londres</li>
</settlement>
<orgName><li>University College de Londres</li>
</orgName>
</list>
<tree><noCountry><name sortKey="Ahmed, Aamir" sort="Ahmed, Aamir" uniqKey="Ahmed A" first="Aamir" last="Ahmed">Aamir Ahmed</name>
<name sortKey="During, Louis" sort="During, Louis" uniqKey="During L" first="Louis" last="Düring">Louis Düring</name>
</noCountry>
<country name="Royaume-Uni"><region name="Angleterre"><name sortKey="Peter, George J" sort="Peter, George J" uniqKey="Peter G" first="George J" last="Peter">George J. Peter</name>
</region>
</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 001796 | SxmlIndent | more

HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 001796 | 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:16407266
   |texte=   Carbon catabolite repression regulates amino acid permeases in Saccharomyces cerevisiae via the TOR signaling pathway.
}}

Pour générer des pages wiki

HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i   -Sk "pubmed:16407266" \
       | HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd   \
       | NlmPubMed2Wicri -a RapamycinFungusV1

This area was generated with Dilib version V0.6.38.
Data generation: Thu Nov 19 21:55:41 2020. Site generation: Thu Nov 19 22:00:39 2020

	Serveur d'exploration sur la rapamycine et les champignons
	Attention, ce site est en cours de développement ! Attention, site généré par des moyens informatiques à partir de corpus bruts. Les informations ne sont donc pas validées.

Serveur d'exploration sur la rapamycine et les champignons

Carbon catabolite repression regulates amino acid permeases in Saccharomyces cerevisiae via the TOR signaling pathway.

Carbon catabolite repression regulates amino acid permeases in Saccharomyces cerevisiae via the TOR signaling pathway.

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki