Feedback regulation of TORC1 by its downstream effectors Npr1 and Par32.
Identifieur interne : 000603 ( Main/Exploration ); précédent : 000602; suivant : 000604Feedback regulation of TORC1 by its downstream effectors Npr1 and Par32.
Auteurs : Natalia V. Varlakhanova [États-Unis] ; Bryan A. Tornabene [États-Unis] ; Marijn G J. Ford [États-Unis]Source :
- Molecular biology of the cell [ 1939-4586 ] ; 2018.
Descripteurs français
- KwdFr :
- Complexe-1 cible mécanistique de la rapamycine (métabolisme), Fractions subcellulaires (métabolisme), Maturation post-traductionnelle des protéines (effets des médicaments et des substances chimiques), Membrane cellulaire (effets des médicaments et des substances chimiques), Membrane cellulaire (métabolisme), Motifs d'acides aminés (MeSH), Mutation (génétique), Noyau de la cellule (effets des médicaments et des substances chimiques), Noyau de la cellule (métabolisme), Protein kinases (métabolisme), Protéines de Saccharomyces cerevisiae (composition chimique), Protéines de Saccharomyces cerevisiae (métabolisme), Rétrocontrôle physiologique (effets des médicaments et des substances chimiques), Saccharomyces cerevisiae (cytologie), Saccharomyces cerevisiae (effets des médicaments et des substances chimiques), Saccharomyces cerevisiae (métabolisme), Sirolimus (pharmacologie), Systèmes de transport d'acides aminés (métabolisme), Séquence conservée (MeSH), Transport des protéines (effets des médicaments et des substances chimiques).
- MESH :
- composition chimique : Protéines de Saccharomyces cerevisiae.
- cytologie : Saccharomyces cerevisiae.
- effets des médicaments et des substances chimiques : Maturation post-traductionnelle des protéines, Membrane cellulaire, Noyau de la cellule, Rétrocontrôle physiologique, Saccharomyces cerevisiae, Transport des protéines.
- génétique : Mutation.
- métabolisme : Complexe-1 cible mécanistique de la rapamycine, Fractions subcellulaires, Membrane cellulaire, Noyau de la cellule, Protein kinases, Protéines de Saccharomyces cerevisiae, Saccharomyces cerevisiae, Systèmes de transport d'acides aminés.
- pharmacologie : Sirolimus.
- Motifs d'acides aminés, Séquence conservée.
English descriptors
- KwdEn :
- Amino Acid Motifs (MeSH), Amino Acid Transport Systems (metabolism), Cell Membrane (drug effects), Cell Membrane (metabolism), Cell Nucleus (drug effects), Cell Nucleus (metabolism), Conserved Sequence (MeSH), Feedback, Physiological (drug effects), Mechanistic Target of Rapamycin Complex 1 (metabolism), Mutation (genetics), Protein Kinases (metabolism), Protein Processing, Post-Translational (drug effects), Protein Transport (drug effects), Saccharomyces cerevisiae (cytology), Saccharomyces cerevisiae (drug effects), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (chemistry), Saccharomyces cerevisiae Proteins (metabolism), Sirolimus (pharmacology), Subcellular Fractions (metabolism).
- MESH :
- chemical , chemistry : Saccharomyces cerevisiae Proteins.
- chemical , metabolism : Amino Acid Transport Systems, Mechanistic Target of Rapamycin Complex 1, Protein Kinases, Saccharomyces cerevisiae Proteins.
- cytology : Saccharomyces cerevisiae.
- drug effects : Cell Membrane, Cell Nucleus, Feedback, Physiological, Protein Processing, Post-Translational, Protein Transport, Saccharomyces cerevisiae.
- genetics : Mutation.
- metabolism : Cell Membrane, Cell Nucleus, Saccharomyces cerevisiae, Subcellular Fractions.
- chemical , pharmacology : Sirolimus.
- Amino Acid Motifs, Conserved Sequence.
Abstract
TORC1 (target of rapamycin complex) integrates complex nutrient signals to generate and fine-tune a growth and metabolic response. Npr1 (nitrogen permease reactivator) is a downstream effector kinase of TORC1 that regulates the stability, activity, and trafficking of various nutrient permeases including the ammonium permeases Mep1, Mep2, and Mep3 and the general amino acid permease Gap1. Npr1 exerts its regulatory effects on Mep1 and Mep3 via Par32 (phosphorylated after rapamycin). Activation of Npr1 leads to phosphorylation of Par32, resulting in changes in its subcellular localization and function. Here we demonstrate that Par32 is a positive regulator of TORC1 activity. Loss of Par32 renders cells unable to recover from exposure to rapamycin and reverses the resistance to rapamycin of Δ npr1 cells. The sensitivity to rapamycin of cells lacking Par32 is dependent on Mep1 and Mep3 and the presence of ammonium, linking ammonium metabolism to TORC1 activity. Par32 function requires its conserved repeated glycine-rich motifs to be intact but, surprisingly, does not require its localization to the plasma membrane. In all, this work elucidates a novel mechanism by which Npr1 and Par32 exert regulatory feedback on TORC1.
DOI: 10.1091/mbc.E18-03-0158
PubMed: 30156471
PubMed Central: PMC6249832
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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kinases</term><term>Protéines de Saccharomyces cerevisiae</term><term>Saccharomyces cerevisiae</term><term>Systèmes de transport d'acides aminés</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>Amino Acid Motifs</term><term>Conserved Sequence</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Motifs d'acides aminés</term><term>Séquence conservée</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">TORC1 (target of rapamycin complex) integrates complex nutrient signals to generate and fine-tune a growth and metabolic response. Npr1 (nitrogen permease reactivator) is a downstream effector kinase of TORC1 that regulates the stability, activity, and trafficking of various nutrient permeases including the ammonium permeases Mep1, Mep2, and Mep3 and the general amino acid permease Gap1. Npr1 exerts its regulatory effects on Mep1 and Mep3 via Par32 (phosphorylated after rapamycin). Activation of Npr1 leads to phosphorylation of Par32, resulting in changes in its subcellular localization and function. Here we demonstrate that Par32 is a positive regulator of TORC1 activity. Loss of Par32 renders cells unable to recover from exposure to rapamycin and reverses the resistance to rapamycin of Δ npr1 cells. The sensitivity to rapamycin of cells lacking Par32 is dependent on Mep1 and Mep3 and the presence of ammonium, linking ammonium metabolism to TORC1 activity. Par32 function requires its conserved repeated glycine-rich motifs to be intact but, surprisingly, does not require its localization to the plasma membrane. In all, this work elucidates a novel mechanism by which Npr1 and Par32 exert regulatory feedback on TORC1.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">30156471</PMID><DateCompleted><Year>2019</Year><Month>05</Month><Day>17</Day></DateCompleted><DateRevised><Year>2019</Year><Month>05</Month><Day>17</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1939-4586</ISSN><JournalIssue CitedMedium="Internet"><Volume>29</Volume><Issue>22</Issue><PubDate><Year>2018</Year><Month>11</Month><Day>01</Day></PubDate></JournalIssue><Title>Molecular biology of the cell</Title><ISOAbbreviation>Mol Biol Cell</ISOAbbreviation></Journal><ArticleTitle>Feedback regulation of TORC1 by its downstream effectors Npr1 and Par32.</ArticleTitle><Pagination><MedlinePgn>2751-2765</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1091/mbc.E18-03-0158</ELocationID><Abstract><AbstractText>TORC1 (target of rapamycin complex) integrates complex nutrient signals to generate and fine-tune a growth and metabolic response. Npr1 (nitrogen permease reactivator) is a downstream effector kinase of TORC1 that regulates the stability, activity, and trafficking of various nutrient permeases including the ammonium permeases Mep1, Mep2, and Mep3 and the general amino acid permease Gap1. Npr1 exerts its regulatory effects on Mep1 and Mep3 via Par32 (phosphorylated after rapamycin). Activation of Npr1 leads to phosphorylation of Par32, resulting in changes in its subcellular localization and function. Here we demonstrate that Par32 is a positive regulator of TORC1 activity. Loss of Par32 renders cells unable to recover from exposure to rapamycin and reverses the resistance to rapamycin of Δ npr1 cells. The sensitivity to rapamycin of cells lacking Par32 is dependent on Mep1 and Mep3 and the presence of ammonium, linking ammonium metabolism to TORC1 activity. Par32 function requires its conserved repeated glycine-rich motifs to be intact but, surprisingly, does not require its localization to the plasma membrane. In all, this work elucidates a novel mechanism by which Npr1 and Par32 exert regulatory feedback on TORC1.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Varlakhanova</LastName><ForeName>Natalia V</ForeName><Initials>NV</Initials><AffiliationInfo><Affiliation>Department of Cell Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA 15261.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Tornabene</LastName><ForeName>Bryan A</ForeName><Initials>BA</Initials><AffiliationInfo><Affiliation>Department of Cell Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA 15261.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ford</LastName><ForeName>Marijn G J</ForeName><Initials>MGJ</Initials><AffiliationInfo><Affiliation>Department of Cell Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA 15261.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01 GM120102</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></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2018</Year><Month>08</Month><Day>29</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Mol Biol Cell</MedlineTA><NlmUniqueID>9201390</NlmUniqueID><ISSNLinking>1059-1524</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D026905">Amino Acid Transport Systems</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C491145">GAP1 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C000607163">Par32 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029701">Saccharomyces cerevisiae Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>147682-31-3</RegistryNumber><NameOfSubstance UI="C066958">NPR1 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.-</RegistryNumber><NameOfSubstance UI="D011494">Protein Kinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber><NameOfSubstance UI="D000076222">Mechanistic Target of Rapamycin Complex 1</NameOfSubstance></Chemical><Chemical><RegistryNumber>W36ZG6FT64</RegistryNumber><NameOfSubstance UI="D020123">Sirolimus</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D020816" MajorTopicYN="N">Amino Acid Motifs</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D026905" MajorTopicYN="N">Amino Acid Transport Systems</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002462" MajorTopicYN="N">Cell Membrane</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002467" MajorTopicYN="N">Cell Nucleus</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017124" MajorTopicYN="N">Conserved Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D025461" MajorTopicYN="Y">Feedback, Physiological</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000076222" MajorTopicYN="N">Mechanistic Target of Rapamycin Complex 1</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011494" MajorTopicYN="N">Protein Kinases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011499" MajorTopicYN="N">Protein Processing, Post-Translational</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D021381" MajorTopicYN="N">Protein Transport</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000166" MajorTopicYN="N">cytology</QualifierName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029701" MajorTopicYN="N">Saccharomyces cerevisiae Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020123" MajorTopicYN="N">Sirolimus</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013347" MajorTopicYN="N">Subcellular Fractions</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate 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Varlakhanova</name></region><name sortKey="Ford, Marijn G J" sort="Ford, Marijn G J" uniqKey="Ford M" first="Marijn G J" last="Ford">Marijn G J. Ford</name><name sortKey="Tornabene, Bryan A" sort="Tornabene, Bryan A" uniqKey="Tornabene B" first="Bryan A" last="Tornabene">Bryan A. Tornabene</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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