mTORC1-independent Raptor prevents hepatic steatosis by stabilizing PHLPP2.
Identifieur interne : 000953 ( Main/Exploration ); précédent : 000952; suivant : 000954mTORC1-independent Raptor prevents hepatic steatosis by stabilizing PHLPP2.
Auteurs : Kyeongjin Kim [États-Unis] ; Li Qiang [États-Unis] ; Matthew S. Hayden [États-Unis] ; David P. Sparling [États-Unis] ; Nicole H. Purcell [États-Unis] ; Utpal B. Pajvani [États-Unis]Source :
- Nature communications [ 2041-1723 ] ; 2016.
Descripteurs français
- KwdFr :
- Alimentation riche en graisse (MeSH), Animaux (MeSH), Chromatographie sur gel (MeSH), Complexe-1 cible mécanistique de la rapamycine (MeSH), Complexes multiprotéiques (MeSH), Foie (métabolisme), Glycémie (métabolisme), Hépatocytes (métabolisme), Immunoprécipitation (MeSH), Insuline (métabolisme), Lipogenèse (génétique), Obésité (génétique), Obésité (métabolisme), Phosphoprotein Phosphatases (métabolisme), Protéine de régulation associée à mTOR (MeSH), Protéine oncogène v-akt (métabolisme), Protéines adaptatrices de la transduction du signal (génétique), Protéines à répétitions de séquences bêta-transducine (métabolisme), RT-PCR (MeSH), Souris (MeSH), Stéatose hépatique (génétique), Stéatose hépatique (métabolisme), Stéatose hépatique non alcoolique (génétique), Stéatose hépatique non alcoolique (métabolisme), Sérine-thréonine kinases TOR (MeSH), Technique de Western (MeSH), Transduction du signal (MeSH), Triglycéride (métabolisme).
- MESH :
- génétique : Lipogenèse, Obésité, Protéines adaptatrices de la transduction du signal, Stéatose hépatique, Stéatose hépatique non alcoolique.
- métabolisme : Foie, Glycémie, Hépatocytes, Insuline, Obésité, Phosphoprotein Phosphatases, Protéine oncogène v-akt, Protéines à répétitions de séquences bêta-transducine, Stéatose hépatique, Stéatose hépatique non alcoolique, Triglycéride.
- Alimentation riche en graisse, Animaux, Chromatographie sur gel, Complexe-1 cible mécanistique de la rapamycine, Complexes multiprotéiques, Immunoprécipitation, Protéine de régulation associée à mTOR, RT-PCR, Souris, Sérine-thréonine kinases TOR, Technique de Western, Transduction du signal.
English descriptors
- KwdEn :
- Adaptor Proteins, Signal Transducing (genetics), Animals (MeSH), Blood Glucose (metabolism), Blotting, Western (MeSH), Chromatography, Gel (MeSH), Diet, High-Fat (MeSH), Fatty Liver (genetics), Fatty Liver (metabolism), Hepatocytes (metabolism), Immunoprecipitation (MeSH), Insulin (metabolism), Lipogenesis (genetics), Liver (metabolism), Mechanistic Target of Rapamycin Complex 1 (MeSH), Mice (MeSH), Multiprotein Complexes (MeSH), Non-alcoholic Fatty Liver Disease (genetics), Non-alcoholic Fatty Liver Disease (metabolism), Obesity (genetics), Obesity (metabolism), Oncogene Protein v-akt (metabolism), Phosphoprotein Phosphatases (metabolism), Regulatory-Associated Protein of mTOR (MeSH), Reverse Transcriptase Polymerase Chain Reaction (MeSH), Signal Transduction (MeSH), TOR Serine-Threonine Kinases (MeSH), Triglycerides (metabolism), beta-Transducin Repeat-Containing Proteins (metabolism).
- MESH :
- chemical , genetics : Adaptor Proteins, Signal Transducing.
- chemical , metabolism : Blood Glucose, Insulin, Oncogene Protein v-akt, Phosphoprotein Phosphatases, Triglycerides, beta-Transducin Repeat-Containing Proteins.
- genetics : Fatty Liver, Lipogenesis, Non-alcoholic Fatty Liver Disease, Obesity.
- metabolism : Fatty Liver, Hepatocytes, Liver, Non-alcoholic Fatty Liver Disease, Obesity.
- Animals, Blotting, Western, Chromatography, Gel, Diet, High-Fat, Immunoprecipitation, Mechanistic Target of Rapamycin Complex 1, Mice, Multiprotein Complexes, Regulatory-Associated Protein of mTOR, Reverse Transcriptase Polymerase Chain Reaction, Signal Transduction, TOR Serine-Threonine Kinases.
Abstract
Mechanistic target of rapamycin complex 1 (mTORC1), defined by the presence of Raptor, is an evolutionarily conserved and nutrient-sensitive regulator of cellular growth and other metabolic processes. To date, all known functions of Raptor involve its scaffolding mTOR kinase with substrate. Here we report that mTORC1-independent ('free') Raptor negatively regulates hepatic Akt activity and lipogenesis. Free Raptor levels in liver decline with age and in obesity; restoration of free Raptor levels reduces liver triglyceride content, through reduced β-TrCP-mediated degradation of the Akt phosphatase, PHLPP2. Commensurately, forced PHLPP2 expression ameliorates hepatic steatosis in diet-induced obese mice. These data suggest that the balance of free and mTORC1-associated Raptor governs hepatic lipid accumulation, and uncover the potentially therapeutic role of PHLPP2 activators in non-alcoholic fatty liver disease.
DOI: 10.1038/ncomms10255
PubMed: 26743335
PubMed Central: PMC4729872
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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<term>Animals (MeSH)</term>
<term>Blood Glucose (metabolism)</term>
<term>Blotting, Western (MeSH)</term>
<term>Chromatography, Gel (MeSH)</term>
<term>Diet, High-Fat (MeSH)</term>
<term>Fatty Liver (genetics)</term>
<term>Fatty Liver (metabolism)</term>
<term>Hepatocytes (metabolism)</term>
<term>Immunoprecipitation (MeSH)</term>
<term>Insulin (metabolism)</term>
<term>Lipogenesis (genetics)</term>
<term>Liver (metabolism)</term>
<term>Mechanistic Target of Rapamycin Complex 1 (MeSH)</term>
<term>Mice (MeSH)</term>
<term>Multiprotein Complexes (MeSH)</term>
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<term>Non-alcoholic Fatty Liver Disease (metabolism)</term>
<term>Obesity (genetics)</term>
<term>Obesity (metabolism)</term>
<term>Oncogene Protein v-akt (metabolism)</term>
<term>Phosphoprotein Phosphatases (metabolism)</term>
<term>Regulatory-Associated Protein of mTOR (MeSH)</term>
<term>Reverse Transcriptase Polymerase Chain Reaction (MeSH)</term>
<term>Signal Transduction (MeSH)</term>
<term>TOR Serine-Threonine Kinases (MeSH)</term>
<term>Triglycerides (metabolism)</term>
<term>beta-Transducin Repeat-Containing Proteins (metabolism)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Alimentation riche en graisse (MeSH)</term>
<term>Animaux (MeSH)</term>
<term>Chromatographie sur gel (MeSH)</term>
<term>Complexe-1 cible mécanistique de la rapamycine (MeSH)</term>
<term>Complexes multiprotéiques (MeSH)</term>
<term>Foie (métabolisme)</term>
<term>Glycémie (métabolisme)</term>
<term>Hépatocytes (métabolisme)</term>
<term>Immunoprécipitation (MeSH)</term>
<term>Insuline (métabolisme)</term>
<term>Lipogenèse (génétique)</term>
<term>Obésité (génétique)</term>
<term>Obésité (métabolisme)</term>
<term>Phosphoprotein Phosphatases (métabolisme)</term>
<term>Protéine de régulation associée à mTOR (MeSH)</term>
<term>Protéine oncogène v-akt (métabolisme)</term>
<term>Protéines adaptatrices de la transduction du signal (génétique)</term>
<term>Protéines à répétitions de séquences bêta-transducine (métabolisme)</term>
<term>RT-PCR (MeSH)</term>
<term>Souris (MeSH)</term>
<term>Stéatose hépatique (génétique)</term>
<term>Stéatose hépatique (métabolisme)</term>
<term>Stéatose hépatique non alcoolique (génétique)</term>
<term>Stéatose hépatique non alcoolique (métabolisme)</term>
<term>Sérine-thréonine kinases TOR (MeSH)</term>
<term>Technique de Western (MeSH)</term>
<term>Transduction du signal (MeSH)</term>
<term>Triglycéride (métabolisme)</term>
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<term>Insulin</term>
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<term>Phosphoprotein Phosphatases</term>
<term>Triglycerides</term>
<term>beta-Transducin Repeat-Containing Proteins</term>
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<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Fatty Liver</term>
<term>Lipogenesis</term>
<term>Non-alcoholic Fatty Liver Disease</term>
<term>Obesity</term>
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<term>Obésité</term>
<term>Protéines adaptatrices de la transduction du signal</term>
<term>Stéatose hépatique</term>
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<term>Hepatocytes</term>
<term>Liver</term>
<term>Non-alcoholic Fatty Liver Disease</term>
<term>Obesity</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Foie</term>
<term>Glycémie</term>
<term>Hépatocytes</term>
<term>Insuline</term>
<term>Obésité</term>
<term>Phosphoprotein Phosphatases</term>
<term>Protéine oncogène v-akt</term>
<term>Protéines à répétitions de séquences bêta-transducine</term>
<term>Stéatose hépatique</term>
<term>Stéatose hépatique non alcoolique</term>
<term>Triglycéride</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
<term>Blotting, Western</term>
<term>Chromatography, Gel</term>
<term>Diet, High-Fat</term>
<term>Immunoprecipitation</term>
<term>Mechanistic Target of Rapamycin Complex 1</term>
<term>Mice</term>
<term>Multiprotein Complexes</term>
<term>Regulatory-Associated Protein of mTOR</term>
<term>Reverse Transcriptase Polymerase Chain Reaction</term>
<term>Signal Transduction</term>
<term>TOR Serine-Threonine Kinases</term>
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<keywords scheme="MESH" xml:lang="fr"><term>Alimentation riche en graisse</term>
<term>Animaux</term>
<term>Chromatographie sur gel</term>
<term>Complexe-1 cible mécanistique de la rapamycine</term>
<term>Complexes multiprotéiques</term>
<term>Immunoprécipitation</term>
<term>Protéine de régulation associée à mTOR</term>
<term>RT-PCR</term>
<term>Souris</term>
<term>Sérine-thréonine kinases TOR</term>
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<front><div type="abstract" xml:lang="en">Mechanistic target of rapamycin complex 1 (mTORC1), defined by the presence of Raptor, is an evolutionarily conserved and nutrient-sensitive regulator of cellular growth and other metabolic processes. To date, all known functions of Raptor involve its scaffolding mTOR kinase with substrate. Here we report that mTORC1-independent ('free') Raptor negatively regulates hepatic Akt activity and lipogenesis. Free Raptor levels in liver decline with age and in obesity; restoration of free Raptor levels reduces liver triglyceride content, through reduced β-TrCP-mediated degradation of the Akt phosphatase, PHLPP2. Commensurately, forced PHLPP2 expression ameliorates hepatic steatosis in diet-induced obese mice. These data suggest that the balance of free and mTORC1-associated Raptor governs hepatic lipid accumulation, and uncover the potentially therapeutic role of PHLPP2 activators in non-alcoholic fatty liver disease. </div>
</front>
</TEI>
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<DateCompleted><Year>2016</Year>
<Month>05</Month>
<Day>17</Day>
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<Month>11</Month>
<Day>13</Day>
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<Day>08</Day>
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<Title>Nature communications</Title>
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<ArticleTitle>mTORC1-independent Raptor prevents hepatic steatosis by stabilizing PHLPP2.</ArticleTitle>
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<Abstract><AbstractText>Mechanistic target of rapamycin complex 1 (mTORC1), defined by the presence of Raptor, is an evolutionarily conserved and nutrient-sensitive regulator of cellular growth and other metabolic processes. To date, all known functions of Raptor involve its scaffolding mTOR kinase with substrate. Here we report that mTORC1-independent ('free') Raptor negatively regulates hepatic Akt activity and lipogenesis. Free Raptor levels in liver decline with age and in obesity; restoration of free Raptor levels reduces liver triglyceride content, through reduced β-TrCP-mediated degradation of the Akt phosphatase, PHLPP2. Commensurately, forced PHLPP2 expression ameliorates hepatic steatosis in diet-induced obese mice. These data suggest that the balance of free and mTORC1-associated Raptor governs hepatic lipid accumulation, and uncover the potentially therapeutic role of PHLPP2 activators in non-alcoholic fatty liver disease. </AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kim</LastName>
<ForeName>KyeongJin</ForeName>
<Initials>K</Initials>
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</AffiliationInfo>
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<ForeName>Li</ForeName>
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</AffiliationInfo>
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<Initials>MS</Initials>
<AffiliationInfo><Affiliation>Department of Dermatology, Columbia University, New York, New York 10032, USA.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Department of Microbiology &Immunology, Columbia University, New York, New York 10032, USA.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Sparling</LastName>
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<AffiliationInfo><Affiliation>Department of Pediatrics, Columbia University, New York, New York 10032, USA.</Affiliation>
</AffiliationInfo>
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<ForeName>Nicole H</ForeName>
<Initials>NH</Initials>
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</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Pajvani</LastName>
<ForeName>Utpal B</ForeName>
<Initials>UB</Initials>
<AffiliationInfo><Affiliation>Department of Medicine, Columbia University, New York, New York 10032, USA.</Affiliation>
</AffiliationInfo>
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<Language>eng</Language>
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<Acronym>DK</Acronym>
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<Country>United States</Country>
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