Target Of Rapamycin pathway in the white-rot fungus Phanerochaete chrysosporium.
Identifieur interne : 000018 ( Main/Exploration ); précédent : 000017; suivant : 000019Target Of Rapamycin pathway in the white-rot fungus Phanerochaete chrysosporium.
Auteurs : Duy Vuong Nguyen [France] ; Thomas Roret [France] ; Antonio Fernandez-Gonzalez [France] ; Annegret Kohler [France] ; Mélanie Morel-Rouhier [France] ; Eric Gelhaye [France] ; Rodnay Sormani [France]Source :
- PloS one [ 1932-6203 ] ; 2020.
Descripteurs français
- KwdFr :
- Humains (MeSH), Liaison hydrogène (MeSH), Phanerochaete (croissance et développement), Phanerochaete (métabolisme), Protéines fongiques (antagonistes et inhibiteurs), Protéines fongiques (métabolisme), Protéome (MeSH), Réaction de polymérisation en chaîne (MeSH), Sirolimus (pharmacologie), Sites de fixation (MeSH), Spores fongiques (métabolisme), Structure secondaire des protéines (MeSH), Sérine-thréonine kinases TOR (antagonistes et inhibiteurs), Sérine-thréonine kinases TOR (métabolisme), Transduction du signal (effets des médicaments et des substances chimiques), bêta-Glucosidase (métabolisme).
- MESH :
- antagonistes et inhibiteurs : Protéines fongiques, Sérine-thréonine kinases TOR.
- croissance et développement : Phanerochaete.
- effets des médicaments et des substances chimiques : Transduction du signal.
- métabolisme : Phanerochaete, Protéines fongiques, Spores fongiques, Sérine-thréonine kinases TOR, bêta-Glucosidase.
- pharmacologie : Sirolimus.
- Humains, Liaison hydrogène, Protéome, Réaction de polymérisation en chaîne, Sites de fixation, Structure secondaire des protéines.
English descriptors
- KwdEn :
- Binding Sites (MeSH), Fungal Proteins (antagonists & inhibitors), Fungal Proteins (metabolism), Humans (MeSH), Hydrogen Bonding (MeSH), Phanerochaete (growth & development), Phanerochaete (metabolism), Polymerase Chain Reaction (MeSH), Protein Structure, Secondary (MeSH), Proteome (MeSH), Signal Transduction (drug effects), Sirolimus (pharmacology), Spores, Fungal (metabolism), TOR Serine-Threonine Kinases (antagonists & inhibitors), TOR Serine-Threonine Kinases (metabolism), beta-Glucosidase (metabolism).
- MESH :
- chemical , antagonists & inhibitors : Fungal Proteins, TOR Serine-Threonine Kinases.
- chemical , metabolism : Fungal Proteins, TOR Serine-Threonine Kinases, beta-Glucosidase.
- drug effects : Signal Transduction.
- growth & development : Phanerochaete.
- metabolism : Phanerochaete, Spores, Fungal.
- chemical , pharmacology : Sirolimus.
- Binding Sites, Humans, Hydrogen Bonding, Polymerase Chain Reaction, Protein Structure, Secondary, Proteome.
Abstract
The Target Of Rapamycin (TOR) signaling pathway is known to regulate growth in response to nutrient availability and stress in eukaryotic cells. In the present study, we have investigated the TOR pathway in the white-rot fungus Phanerochaete chrysosporium. Inhibition of TOR activity by rapamycin affects conidia germination and hyphal growth highlighting the conserved mechanism of susceptibility to rapamycin. Interestingly, the secreted protein content is also affected by the rapamycin treatment. Finally, homologs of the components of TOR pathway can be identified in P. chrysosporium. Altogether, those results indicate that the TOR pathway of P. chrysosporium plays a central role in this fungus.
DOI: 10.1371/journal.pone.0224776
PubMed: 32078630
PubMed Central: PMC7032718
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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last="Nguyen">Duy Vuong Nguyen</name><affiliation wicri:level="4"><nlm:affiliation>Université de Lorraine, INRA, IAM, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Université de Lorraine, INRA, IAM</wicri:regionArea><wicri:noRegion>IAM</wicri:noRegion><orgName type="university">Université de Lorraine</orgName><placeName><settlement type="city">Nancy</settlement><settlement type="city">Metz</settlement><region type="region" nuts="2">Grand Est</region><region type="old region" nuts="2">Lorraine (région)</region></placeName></affiliation></author><author><name sortKey="Roret, Thomas" sort="Roret, Thomas" uniqKey="Roret T" first="Thomas" last="Roret">Thomas Roret</name><affiliation wicri:level="4"><nlm:affiliation>Université de Lorraine, INRA, IAM, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Université de Lorraine, INRA, IAM</wicri:regionArea><wicri:noRegion>IAM</wicri:noRegion><orgName type="university">Université 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(région)</region></placeName></affiliation></author><author><name sortKey="Kohler, Annegret" sort="Kohler, Annegret" uniqKey="Kohler A" first="Annegret" last="Kohler">Annegret Kohler</name><affiliation wicri:level="4"><nlm:affiliation>Université de Lorraine, INRA, IAM, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Université de Lorraine, INRA, IAM</wicri:regionArea><wicri:noRegion>IAM</wicri:noRegion><orgName type="university">Université de Lorraine</orgName><placeName><settlement type="city">Nancy</settlement><settlement type="city">Metz</settlement><region type="region" nuts="2">Grand Est</region><region type="old region" nuts="2">Lorraine (région)</region></placeName></affiliation></author><author><name sortKey="Morel Rouhier, Melanie" sort="Morel Rouhier, Melanie" uniqKey="Morel Rouhier M" first="Mélanie" last="Morel-Rouhier">Mélanie Morel-Rouhier</name><affiliation wicri:level="4"><nlm:affiliation>Université de Lorraine, INRA, IAM, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Université de Lorraine, INRA, IAM</wicri:regionArea><wicri:noRegion>IAM</wicri:noRegion><orgName type="university">Université de Lorraine</orgName><placeName><settlement type="city">Nancy</settlement><settlement type="city">Metz</settlement><region type="region" nuts="2">Grand Est</region><region type="old region" nuts="2">Lorraine (région)</region></placeName></affiliation></author><author><name sortKey="Gelhaye, Eric" sort="Gelhaye, Eric" uniqKey="Gelhaye E" first="Eric" last="Gelhaye">Eric Gelhaye</name><affiliation wicri:level="4"><nlm:affiliation>Université de Lorraine, INRA, IAM, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Université de Lorraine, INRA, IAM</wicri:regionArea><wicri:noRegion>IAM</wicri:noRegion><orgName type="university">Université de Lorraine</orgName><placeName><settlement type="city">Nancy</settlement><settlement type="city">Metz</settlement><region type="region" nuts="2">Grand Est</region><region type="old region" nuts="2">Lorraine (région)</region></placeName></affiliation></author><author><name sortKey="Sormani, Rodnay" sort="Sormani, Rodnay" uniqKey="Sormani R" first="Rodnay" last="Sormani">Rodnay Sormani</name><affiliation wicri:level="4"><nlm:affiliation>Université de Lorraine, INRA, IAM, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Université de Lorraine, INRA, IAM</wicri:regionArea><wicri:noRegion>IAM</wicri:noRegion><orgName type="university">Université de Lorraine</orgName><placeName><settlement type="city">Nancy</settlement><settlement type="city">Metz</settlement><region type="region" nuts="2">Grand Est</region><region type="old region" nuts="2">Lorraine (région)</region></placeName></affiliation></author></analytic><series><title level="j">PloS one</title><idno type="eISSN">1932-6203</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Binding Sites (MeSH)</term><term>Fungal Proteins (antagonists & inhibitors)</term><term>Fungal Proteins (metabolism)</term><term>Humans (MeSH)</term><term>Hydrogen Bonding (MeSH)</term><term>Phanerochaete (growth & development)</term><term>Phanerochaete (metabolism)</term><term>Polymerase Chain Reaction (MeSH)</term><term>Protein Structure, Secondary (MeSH)</term><term>Proteome (MeSH)</term><term>Signal Transduction (drug effects)</term><term>Sirolimus (pharmacology)</term><term>Spores, Fungal (metabolism)</term><term>TOR Serine-Threonine Kinases (antagonists & inhibitors)</term><term>TOR Serine-Threonine Kinases (metabolism)</term><term>beta-Glucosidase (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Humains (MeSH)</term><term>Liaison hydrogène (MeSH)</term><term>Phanerochaete (croissance et développement)</term><term>Phanerochaete (métabolisme)</term><term>Protéines fongiques (antagonistes et inhibiteurs)</term><term>Protéines fongiques (métabolisme)</term><term>Protéome (MeSH)</term><term>Réaction de polymérisation en chaîne (MeSH)</term><term>Sirolimus (pharmacologie)</term><term>Sites de fixation (MeSH)</term><term>Spores fongiques (métabolisme)</term><term>Structure secondaire des protéines (MeSH)</term><term>Sérine-thréonine kinases TOR (antagonistes et inhibiteurs)</term><term>Sérine-thréonine kinases TOR (métabolisme)</term><term>Transduction du signal (effets des médicaments et des substances chimiques)</term><term>bêta-Glucosidase (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Fungal Proteins</term><term>TOR Serine-Threonine Kinases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Fungal Proteins</term><term>TOR Serine-Threonine Kinases</term><term>beta-Glucosidase</term></keywords><keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Protéines fongiques</term><term>Sérine-thréonine kinases TOR</term></keywords><keywords scheme="MESH" qualifier="croissance et développement" xml:lang="fr"><term>Phanerochaete</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Signal Transduction</term></keywords><keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Transduction du signal</term></keywords><keywords scheme="MESH" qualifier="growth & development" xml:lang="en"><term>Phanerochaete</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Phanerochaete</term><term>Spores, Fungal</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Phanerochaete</term><term>Protéines fongiques</term><term>Spores fongiques</term><term>Sérine-thréonine kinases TOR</term><term>bêta-Glucosidase</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Sirolimus</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Sirolimus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Binding Sites</term><term>Humans</term><term>Hydrogen Bonding</term><term>Polymerase Chain Reaction</term><term>Protein Structure, Secondary</term><term>Proteome</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Humains</term><term>Liaison hydrogène</term><term>Protéome</term><term>Réaction de polymérisation en chaîne</term><term>Sites de fixation</term><term>Structure secondaire des protéines</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The Target Of Rapamycin (TOR) signaling pathway is known to regulate growth in response to nutrient availability and stress in eukaryotic cells. In the present study, we have investigated the TOR pathway in the white-rot fungus Phanerochaete chrysosporium. Inhibition of TOR activity by rapamycin affects conidia germination and hyphal growth highlighting the conserved mechanism of susceptibility to rapamycin. Interestingly, the secreted protein content is also affected by the rapamycin treatment. Finally, homologs of the components of TOR pathway can be identified in P. chrysosporium. Altogether, those results indicate that the TOR pathway of P. chrysosporium plays a central role in this fungus.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">32078630</PMID><DateCompleted><Year>2020</Year><Month>05</Month><Day>05</Day></DateCompleted><DateRevised><Year>2020</Year><Month>05</Month><Day>05</Day></DateRevised><Article PubModel="Electronic-eCollection"><Journal><ISSN IssnType="Electronic">1932-6203</ISSN><JournalIssue CitedMedium="Internet"><Volume>15</Volume><Issue>2</Issue><PubDate><Year>2020</Year></PubDate></JournalIssue><Title>PloS one</Title><ISOAbbreviation>PLoS One</ISOAbbreviation></Journal><ArticleTitle>Target Of Rapamycin pathway in the white-rot fungus Phanerochaete chrysosporium.</ArticleTitle><Pagination><MedlinePgn>e0224776</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1371/journal.pone.0224776</ELocationID><Abstract><AbstractText>The Target Of Rapamycin (TOR) signaling pathway is known to regulate growth in response to nutrient availability and stress in eukaryotic cells. In the present study, we have investigated the TOR pathway in the white-rot fungus Phanerochaete chrysosporium. Inhibition of TOR activity by rapamycin affects conidia germination and hyphal growth highlighting the conserved mechanism of susceptibility to rapamycin. Interestingly, the secreted protein content is also affected by the rapamycin treatment. Finally, homologs of the components of TOR pathway can be identified in P. chrysosporium. Altogether, those results indicate that the TOR pathway of P. chrysosporium plays a central role in this fungus.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Nguyen</LastName><ForeName>Duy Vuong</ForeName><Initials>DV</Initials><AffiliationInfo><Affiliation>Université de Lorraine, INRA, IAM, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Roret</LastName><ForeName>Thomas</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Université de Lorraine, INRA, IAM, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Fernandez-Gonzalez</LastName><ForeName>Antonio</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Université de Lorraine, INRA, IAM, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kohler</LastName><ForeName>Annegret</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Université de Lorraine, INRA, IAM, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Morel-Rouhier</LastName><ForeName>Mélanie</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Université de Lorraine, INRA, IAM, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Gelhaye</LastName><ForeName>Eric</ForeName><Initials>E</Initials><AffiliationInfo><Affiliation>Université de Lorraine, INRA, IAM, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sormani</LastName><ForeName>Rodnay</ForeName><Initials>R</Initials><Identifier Source="ORCID">0000-0002-0939-8639</Identifier><AffiliationInfo><Affiliation>Université de Lorraine, INRA, IAM, France.</Affiliation></AffiliationInfo></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>2020</Year><Month>02</Month><Day>20</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>PLoS One</MedlineTA><NlmUniqueID>101285081</NlmUniqueID><ISSNLinking>1932-6203</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D020543">Proteome</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.1.1</RegistryNumber><NameOfSubstance UI="D058570">TOR Serine-Threonine Kinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.21</RegistryNumber><NameOfSubstance UI="D001617">beta-Glucosidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>W36ZG6FT64</RegistryNumber><NameOfSubstance UI="D020123">Sirolimus</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006860" MajorTopicYN="N">Hydrogen Bonding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020075" MajorTopicYN="N">Phanerochaete</DescriptorName><QualifierName UI="Q000254" MajorTopicYN="Y">growth & development</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016133" MajorTopicYN="N">Polymerase Chain Reaction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017433" MajorTopicYN="N">Protein Structure, Secondary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020543" MajorTopicYN="N">Proteome</DescriptorName></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="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013172" MajorTopicYN="N">Spores, Fungal</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D058570" MajorTopicYN="N">TOR Serine-Threonine Kinases</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001617" MajorTopicYN="N">beta-Glucosidase</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList><CoiStatement>The authors have declared that no competing interests exist.</CoiStatement></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2019</Year><Month>10</Month><Day>18</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2020</Year><Month>01</Month><Day>28</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2020</Year><Month>2</Month><Day>21</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2020</Year><Month>2</Month><Day>23</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>5</Month><Day>6</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>epublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">32078630</ArticleId><ArticleId 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name="Grand Est"><name sortKey="Nguyen, Duy Vuong" sort="Nguyen, Duy Vuong" uniqKey="Nguyen D" first="Duy Vuong" last="Nguyen">Duy Vuong Nguyen</name></region><name sortKey="Fernandez Gonzalez, Antonio" sort="Fernandez Gonzalez, Antonio" uniqKey="Fernandez Gonzalez A" first="Antonio" last="Fernandez-Gonzalez">Antonio Fernandez-Gonzalez</name><name sortKey="Gelhaye, Eric" sort="Gelhaye, Eric" uniqKey="Gelhaye E" first="Eric" last="Gelhaye">Eric Gelhaye</name><name sortKey="Kohler, Annegret" sort="Kohler, Annegret" uniqKey="Kohler A" first="Annegret" last="Kohler">Annegret Kohler</name><name sortKey="Morel Rouhier, Melanie" sort="Morel Rouhier, Melanie" uniqKey="Morel Rouhier M" first="Mélanie" last="Morel-Rouhier">Mélanie Morel-Rouhier</name><name sortKey="Roret, Thomas" sort="Roret, Thomas" uniqKey="Roret T" first="Thomas" last="Roret">Thomas Roret</name><name sortKey="Sormani, Rodnay" sort="Sormani, Rodnay" uniqKey="Sormani R" first="Rodnay" last="Sormani">Rodnay 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