RapamycinFungusV1, Main, Exploration, bibRecord, 000774

Phosphate is the third nutrient monitored by TOR in Candida albicans and provides a target for fungal-specific indirect TOR inhibition.

Identifieur interne : 000774 ( Main/Exploration ); précédent : 000773; suivant : 000775

Phosphate is the third nutrient monitored by TOR in Candida albicans and provides a target for fungal-specific indirect TOR inhibition.

Auteurs : Ning-Ning Liu [États-Unis] ; Peter R. Flanagan [Irlande (pays)] ; Jumei Zeng [États-Unis] ; Niketa M. Jani [États-Unis] ; Maria E. Cardenas [États-Unis] ; Gary P. Moran [Irlande (pays)] ; Julia R. Köhler [États-Unis]

Source :

Proceedings of the National Academy of Sciences of the United States of America [ 1091-6490 ] ; 2017.

RBID : pubmed:28566496

Descripteurs français

KwdFr :
- Antifongiques (pharmacologie), Candida albicans (effets des médicaments et des substances chimiques), Candida albicans (génétique), Candida albicans (métabolisme), Complexe-1 cible mécanistique de la rapamycine (antagonistes et inhibiteurs), Complexe-1 cible mécanistique de la rapamycine (génétique), Complexe-1 cible mécanistique de la rapamycine (métabolisme), Délétion de gène (MeSH), Gènes fongiques (MeSH), Hyphae (croissance et développement), Hyphae (génétique), Modèles biologiques (MeSH), Mutation (MeSH), Phosphates (métabolisme), Protéines G monomériques (génétique), Protéines G monomériques (métabolisme), Protéines de Saccharomyces cerevisiae (génétique), Protéines de Saccharomyces cerevisiae (métabolisme), Protéines fongiques (antagonistes et inhibiteurs), Protéines fongiques (génétique), Protéines fongiques (métabolisme), Régulon (MeSH), Symporteurs des ions proton-phosphate (antagonistes et inhibiteurs), Symporteurs des ions proton-phosphate (génétique), Symporteurs des ions proton-phosphate (métabolisme), Transduction du signal (MeSH).
MESH :
- antagonistes et inhibiteurs : Complexe-1 cible mécanistique de la rapamycine, Protéines fongiques, Symporteurs des ions proton-phosphate.
- croissance et développement : Hyphae.
- effets des médicaments et des substances chimiques : Candida albicans.
- génétique : Candida albicans, Complexe-1 cible mécanistique de la rapamycine, Hyphae, Protéines G monomériques, Protéines de Saccharomyces cerevisiae, Protéines fongiques, Symporteurs des ions proton-phosphate.
- métabolisme : Candida albicans, Complexe-1 cible mécanistique de la rapamycine, Phosphates, Protéines G monomériques, Protéines de Saccharomyces cerevisiae, Protéines fongiques, Symporteurs des ions proton-phosphate.
- pharmacologie : Antifongiques.
- Délétion de gène, Gènes fongiques, Modèles biologiques, Mutation, Régulon, Transduction du signal.

English descriptors

KwdEn :
- Antifungal Agents (pharmacology), Candida albicans (drug effects), Candida albicans (genetics), Candida albicans (metabolism), Fungal Proteins (antagonists & inhibitors), Fungal Proteins (genetics), Fungal Proteins (metabolism), Gene Deletion (MeSH), Genes, Fungal (MeSH), Hyphae (genetics), Hyphae (growth & development), Mechanistic Target of Rapamycin Complex 1 (antagonists & inhibitors), Mechanistic Target of Rapamycin Complex 1 (genetics), Mechanistic Target of Rapamycin Complex 1 (metabolism), Models, Biological (MeSH), Monomeric GTP-Binding Proteins (genetics), Monomeric GTP-Binding Proteins (metabolism), Mutation (MeSH), Phosphates (metabolism), Proton-Phosphate Symporters (antagonists & inhibitors), Proton-Phosphate Symporters (genetics), Proton-Phosphate Symporters (metabolism), Regulon (MeSH), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism), Signal Transduction (MeSH).
MESH :
- chemical , antagonists & inhibitors : Fungal Proteins, Mechanistic Target of Rapamycin Complex 1, Proton-Phosphate Symporters.
- chemical , genetics : Fungal Proteins, Mechanistic Target of Rapamycin Complex 1, Monomeric GTP-Binding Proteins, Proton-Phosphate Symporters, Saccharomyces cerevisiae Proteins.
- chemical , metabolism : Fungal Proteins, Mechanistic Target of Rapamycin Complex 1, Monomeric GTP-Binding Proteins, Phosphates, Proton-Phosphate Symporters, Saccharomyces cerevisiae Proteins.
- chemical , pharmacology : Antifungal Agents.
- drug effects : Candida albicans.
- genetics : Candida albicans, Hyphae.
- growth & development : Hyphae.
- metabolism : Candida albicans.
- Gene Deletion, Genes, Fungal, Models, Biological, Mutation, Regulon, Signal Transduction.

Abstract

The Target of Rapamycin (TOR) pathway regulates morphogenesis and responses to host cells in the fungal pathogen Candida albicans Eukaryotic Target of Rapamycin complex 1 (TORC1) induces growth and proliferation in response to nitrogen and carbon source availability. Our unbiased genetic approach seeking unknown components of TORC1 signaling in C. albicans revealed that the phosphate transporter Pho84 is required for normal TORC1 activity. We found that mutants in PHO84 are hypersensitive to rapamycin and in response to phosphate feeding, generate less phosphorylated ribosomal protein S6 (P-S6) than the WT. The small GTPase Gtr1, a component of the TORC1-activating EGO complex, links Pho84 to TORC1. Mutants in Gtr1 but not in another TORC1-activating GTPase, Rhb1, are defective in the P-S6 response to phosphate. Overexpression of Gtr1 and a constitutively active Gtr1^Q67L mutant suppresses TORC1-related defects. In Saccharomyces cerevisiae pho84 mutants, constitutively active Gtr1 suppresses a TORC1 signaling defect but does not rescue rapamycin hypersensitivity. Hence, connections from phosphate homeostasis (PHO) to TORC1 may differ between C. albicans and S. cerevisiae The converse direction of signaling from TORC1 to the PHO regulon previously observed in S. cerevisiae was genetically shown in C. albicans using conditional TOR1 alleles. A small molecule inhibitor of Pho84, a Food and Drug Administration-approved drug, inhibits TORC1 signaling and potentiates the activity of the antifungals amphotericin B and micafungin. Anabolic TORC1-dependent processes require significant amounts of phosphate. Our study shows that phosphate availability is monitored and also controlled by TORC1 and that TORC1 can be indirectly targeted by inhibiting Pho84.

DOI: 10.1073/pnas.1617799114
PubMed: 28566496
PubMed Central: PMC5474788

Affiliations:

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Le document en format XML

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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Antifungal Agents (pharmacology)</term>
<term>Candida albicans (drug effects)</term>
<term>Candida albicans (genetics)</term>
<term>Candida albicans (metabolism)</term>
<term>Fungal Proteins (antagonists & inhibitors)</term>
<term>Fungal Proteins (genetics)</term>
<term>Fungal Proteins (metabolism)</term>
<term>Gene Deletion (MeSH)</term>
<term>Genes, Fungal (MeSH)</term>
<term>Hyphae (genetics)</term>
<term>Hyphae (growth & development)</term>
<term>Mechanistic Target of Rapamycin Complex 1 (antagonists & inhibitors)</term>
<term>Mechanistic Target of Rapamycin Complex 1 (genetics)</term>
<term>Mechanistic Target of Rapamycin Complex 1 (metabolism)</term>
<term>Models, Biological (MeSH)</term>
<term>Monomeric GTP-Binding Proteins (genetics)</term>
<term>Monomeric GTP-Binding Proteins (metabolism)</term>
<term>Mutation (MeSH)</term>
<term>Phosphates (metabolism)</term>
<term>Proton-Phosphate Symporters (antagonists & inhibitors)</term>
<term>Proton-Phosphate Symporters (genetics)</term>
<term>Proton-Phosphate Symporters (metabolism)</term>
<term>Regulon (MeSH)</term>
<term>Saccharomyces cerevisiae Proteins (genetics)</term>
<term>Saccharomyces cerevisiae Proteins (metabolism)</term>
<term>Signal Transduction (MeSH)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Antifongiques (pharmacologie)</term>
<term>Candida albicans (effets des médicaments et des substances chimiques)</term>
<term>Candida albicans (génétique)</term>
<term>Candida albicans (métabolisme)</term>
<term>Complexe-1 cible mécanistique de la rapamycine (antagonistes et inhibiteurs)</term>
<term>Complexe-1 cible mécanistique de la rapamycine (génétique)</term>
<term>Complexe-1 cible mécanistique de la rapamycine (métabolisme)</term>
<term>Délétion de gène (MeSH)</term>
<term>Gènes fongiques (MeSH)</term>
<term>Hyphae (croissance et développement)</term>
<term>Hyphae (génétique)</term>
<term>Modèles biologiques (MeSH)</term>
<term>Mutation (MeSH)</term>
<term>Phosphates (métabolisme)</term>
<term>Protéines G monomériques (génétique)</term>
<term>Protéines G monomériques (métabolisme)</term>
<term>Protéines de Saccharomyces cerevisiae (génétique)</term>
<term>Protéines de Saccharomyces cerevisiae (métabolisme)</term>
<term>Protéines fongiques (antagonistes et inhibiteurs)</term>
<term>Protéines fongiques (génétique)</term>
<term>Protéines fongiques (métabolisme)</term>
<term>Régulon (MeSH)</term>
<term>Symporteurs des ions proton-phosphate (antagonistes et inhibiteurs)</term>
<term>Symporteurs des ions proton-phosphate (génétique)</term>
<term>Symporteurs des ions proton-phosphate (métabolisme)</term>
<term>Transduction du signal (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Fungal Proteins</term>
<term>Mechanistic Target of Rapamycin Complex 1</term>
<term>Proton-Phosphate Symporters</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Fungal Proteins</term>
<term>Mechanistic Target of Rapamycin Complex 1</term>
<term>Monomeric GTP-Binding Proteins</term>
<term>Proton-Phosphate Symporters</term>
<term>Saccharomyces cerevisiae Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Fungal Proteins</term>
<term>Mechanistic Target of Rapamycin Complex 1</term>
<term>Monomeric GTP-Binding Proteins</term>
<term>Phosphates</term>
<term>Proton-Phosphate Symporters</term>
<term>Saccharomyces cerevisiae Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Antifungal Agents</term>
</keywords>
<keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Complexe-1 cible mécanistique de la rapamycine</term>
<term>Protéines fongiques</term>
<term>Symporteurs des ions proton-phosphate</term>
</keywords>
<keywords scheme="MESH" qualifier="croissance et développement" xml:lang="fr"><term>Hyphae</term>
</keywords>
<keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Candida albicans</term>
</keywords>
<keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Candida albicans</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Candida albicans</term>
<term>Hyphae</term>
</keywords>
<keywords scheme="MESH" qualifier="growth & development" xml:lang="en"><term>Hyphae</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Candida albicans</term>
<term>Complexe-1 cible mécanistique de la rapamycine</term>
<term>Hyphae</term>
<term>Protéines G monomériques</term>
<term>Protéines de Saccharomyces cerevisiae</term>
<term>Protéines fongiques</term>
<term>Symporteurs des ions proton-phosphate</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Candida albicans</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Candida albicans</term>
<term>Complexe-1 cible mécanistique de la rapamycine</term>
<term>Phosphates</term>
<term>Protéines G monomériques</term>
<term>Protéines de Saccharomyces cerevisiae</term>
<term>Protéines fongiques</term>
<term>Symporteurs des ions proton-phosphate</term>
</keywords>
<keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Antifongiques</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Gene Deletion</term>
<term>Genes, Fungal</term>
<term>Models, Biological</term>
<term>Mutation</term>
<term>Regulon</term>
<term>Signal Transduction</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Délétion de gène</term>
<term>Gènes fongiques</term>
<term>Modèles biologiques</term>
<term>Mutation</term>
<term>Régulon</term>
<term>Transduction du signal</term>
</keywords>
</textClass>
</profileDesc>
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<front><div type="abstract" xml:lang="en">The Target of Rapamycin (TOR) pathway regulates morphogenesis and responses to host cells in the fungal pathogen <i>Candida albicans</i>
 Eukaryotic Target of Rapamycin complex 1 (TORC1) induces growth and proliferation in response to nitrogen and carbon source availability. Our unbiased genetic approach seeking unknown components of TORC1 signaling in <i>C. albicans</i>
 revealed that the phosphate transporter Pho84 is required for normal TORC1 activity. We found that mutants in <i>PHO84</i>
 are hypersensitive to rapamycin and in response to phosphate feeding, generate less phosphorylated ribosomal protein S6 (P-S6) than the WT. The small GTPase Gtr1, a component of the TORC1-activating EGO complex, links Pho84 to TORC1. Mutants in Gtr1 but not in another TORC1-activating GTPase, Rhb1, are defective in the P-S6 response to phosphate. Overexpression of Gtr1 and a constitutively active Gtr1<sup>Q67L</sup>
 mutant suppresses TORC1-related defects. In <i>Saccharomyces cerevisiae pho84</i>
 mutants, constitutively active Gtr1 suppresses a TORC1 signaling defect but does not rescue rapamycin hypersensitivity. Hence, connections from phosphate homeostasis (PHO) to TORC1 may differ between <i>C. albicans</i>
 and <i>S. cerevisiae</i>
 The converse direction of signaling from TORC1 to the PHO regulon previously observed in <i>S. cerevisiae</i>
 was genetically shown in <i>C. albicans</i>
 using conditional <i>TOR1</i>
 alleles. A small molecule inhibitor of Pho84, a Food and Drug Administration-approved drug, inhibits TORC1 signaling and potentiates the activity of the antifungals amphotericin B and micafungin. Anabolic TORC1-dependent processes require significant amounts of phosphate. Our study shows that phosphate availability is monitored and also controlled by TORC1 and that TORC1 can be indirectly targeted by inhibiting Pho84.</div>
</front>
</TEI>
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<Month>05</Month>
<Day>14</Day>
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<Month>11</Month>
<Day>13</Day>
</DateRevised>
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<JournalIssue CitedMedium="Internet"><Volume>114</Volume>
<Issue>24</Issue>
<PubDate><Year>2017</Year>
<Month>06</Month>
<Day>13</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>Phosphate is the third nutrient monitored by TOR in <i>Candida albicans</i>
 and provides a target for fungal-specific indirect TOR inhibition.</ArticleTitle>
<Pagination><MedlinePgn>6346-6351</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1073/pnas.1617799114</ELocationID>
<Abstract><AbstractText>The Target of Rapamycin (TOR) pathway regulates morphogenesis and responses to host cells in the fungal pathogen <i>Candida albicans</i>
 Eukaryotic Target of Rapamycin complex 1 (TORC1) induces growth and proliferation in response to nitrogen and carbon source availability. Our unbiased genetic approach seeking unknown components of TORC1 signaling in <i>C. albicans</i>
 revealed that the phosphate transporter Pho84 is required for normal TORC1 activity. We found that mutants in <i>PHO84</i>
 are hypersensitive to rapamycin and in response to phosphate feeding, generate less phosphorylated ribosomal protein S6 (P-S6) than the WT. The small GTPase Gtr1, a component of the TORC1-activating EGO complex, links Pho84 to TORC1. Mutants in Gtr1 but not in another TORC1-activating GTPase, Rhb1, are defective in the P-S6 response to phosphate. Overexpression of Gtr1 and a constitutively active Gtr1<sup>Q67L</sup>
 mutant suppresses TORC1-related defects. In <i>Saccharomyces cerevisiae pho84</i>
 mutants, constitutively active Gtr1 suppresses a TORC1 signaling defect but does not rescue rapamycin hypersensitivity. Hence, connections from phosphate homeostasis (PHO) to TORC1 may differ between <i>C. albicans</i>
 and <i>S. cerevisiae</i>
 The converse direction of signaling from TORC1 to the PHO regulon previously observed in <i>S. cerevisiae</i>
 was genetically shown in <i>C. albicans</i>
 using conditional <i>TOR1</i>
 alleles. A small molecule inhibitor of Pho84, a Food and Drug Administration-approved drug, inhibits TORC1 signaling and potentiates the activity of the antifungals amphotericin B and micafungin. Anabolic TORC1-dependent processes require significant amounts of phosphate. Our study shows that phosphate availability is monitored and also controlled by TORC1 and that TORC1 can be indirectly targeted by inhibiting Pho84.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Liu</LastName>
<ForeName>Ning-Ning</ForeName>
<Initials>NN</Initials>
<AffiliationInfo><Affiliation>Boston Children's Hospital and Harvard Medical School, Boston, MA 02115.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Flanagan</LastName>
<ForeName>Peter R</ForeName>
<Initials>PR</Initials>
<AffiliationInfo><Affiliation>Division of Oral Biosciences, School of Dental Science, Trinity College Dublin, Dublin 2, Ireland.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Zeng</LastName>
<ForeName>Jumei</ForeName>
<Initials>J</Initials>
<AffiliationInfo><Affiliation>Boston Children's Hospital and Harvard Medical School, Boston, MA 02115.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Jani</LastName>
<ForeName>Niketa M</ForeName>
<Initials>NM</Initials>
<AffiliationInfo><Affiliation>Boston Children's Hospital and Harvard Medical School, Boston, MA 02115.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Cardenas</LastName>
<ForeName>Maria E</ForeName>
<Initials>ME</Initials>
<AffiliationInfo><Affiliation>Department of Molecular Genetics and Microbiology, Duke University Medical Center, Durham, NC 27710.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Moran</LastName>
<ForeName>Gary P</ForeName>
<Initials>GP</Initials>
<AffiliationInfo><Affiliation>Division of Oral Biosciences, School of Dental Science, Trinity College Dublin, Dublin 2, Ireland.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Köhler</LastName>
<ForeName>Julia R</ForeName>
<Initials>JR</Initials>
<AffiliationInfo><Affiliation>Boston Children's Hospital and Harvard Medical School, Boston, MA 02115; julia.koehler@childrens.harvard.edu.</Affiliation>
</AffiliationInfo>
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<Language>eng</Language>
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<Acronym>AI</Acronym>
<Agency>NIAID NIH HHS</Agency>
<Country>United States</Country>
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<Acronym>CA</Acronym>
<Agency>NCI NIH HHS</Agency>
<Country>United States</Country>
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<Acronym>AI</Acronym>
<Agency>NIAID NIH HHS</Agency>
<Country>United States</Country>
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<ArticleDate DateType="Electronic"><Year>2017</Year>
<Month>05</Month>
<Day>31</Day>
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<MedlineTA>Proc Natl Acad Sci U S A</MedlineTA>
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<ISSNLinking>0027-8424</ISSNLinking>
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<NameOfSubstance UI="D020559">Monomeric GTP-Binding Proteins</NameOfSubstance>
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</MeshHeading>
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<QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName>
<QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D017353" MajorTopicYN="N">Gene Deletion</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D005800" MajorTopicYN="N">Genes, Fungal</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D025301" MajorTopicYN="N">Hyphae</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000254" MajorTopicYN="N">growth & development</QualifierName>
</MeshHeading>
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<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008954" MajorTopicYN="N">Models, Biological</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D020559" MajorTopicYN="N">Monomeric GTP-Binding Proteins</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="D010710" MajorTopicYN="N">Phosphates</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
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<MeshHeading><DescriptorName UI="D028081" MajorTopicYN="N">Proton-Phosphate Symporters</DescriptorName>
<QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D018085" MajorTopicYN="N">Regulon</DescriptorName>
</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>
</MeshHeading>
</MeshHeadingList>
<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">amphotericin B</Keyword>
<Keyword MajorTopicYN="Y">antifungal</Keyword>
<Keyword MajorTopicYN="Y">drug potentiation</Keyword>
<Keyword MajorTopicYN="Y">echinocandin</Keyword>
<Keyword MajorTopicYN="Y">ribosomal protein S6 phosphorylation</Keyword>
</KeywordList>
<CoiStatement>The authors declare no conflict of interest.</CoiStatement>
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	Serveur d'exploration sur la rapamycine et les champignons
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Serveur d'exploration sur la rapamycine et les champignons

Phosphate is the third nutrient monitored by TOR in Candida albicans and provides a target for fungal-specific indirect TOR inhibition.

Phosphate is the third nutrient monitored by TOR in Candida albicans and provides a target for fungal-specific indirect TOR inhibition.

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