RapamycinFungusV1, Main, Exploration, bibRecord, 001A23

A phosphatidylinositol 3-kinase/Akt/mTOR pathway mediates and PTEN antagonizes tumor necrosis factor inhibition of insulin signaling through insulin receptor substrate-1.

Identifieur interne : 001A23 ( Main/Exploration ); précédent : 001A22; suivant : 001A24

A phosphatidylinositol 3-kinase/Akt/mTOR pathway mediates and PTEN antagonizes tumor necrosis factor inhibition of insulin signaling through insulin receptor substrate-1.

Auteurs : O N Ozes [États-Unis] ; H. Akca ; L D Mayo ; J A Gustin ; T. Maehama ; J E Dixon ; D B Donner

Source :

Proceedings of the National Academy of Sciences of the United States of America [ 0027-8424 ] ; 2001.

RBID : pubmed:11287630

Descripteurs français

English descriptors

Abstract

Tyrosine phosphorylation of insulin receptor substrate-1 (IRS-1) by the insulin receptor permits this docking protein to interact with signaling proteins that promote insulin action. Serine phosphorylation uncouples IRS-1 from the insulin receptor, thereby inhibiting its tyrosine phosphorylation and insulin signaling. For this reason, there is great interest in identifying serine/threonine kinases for which IRS-1 is a substrate. Tumor necrosis factor (TNF) inhibited insulin-promoted tyrosine phosphorylation of IRS-1 and activated the Akt/protein kinase B serine-threonine kinase, a downstream target for phosphatidylinositol 3-kinase (PI 3-kinase). The effect of TNF on insulin-promoted tyrosine phosphorylation of IRS-1 was blocked by inhibition of PI 3-kinase and the PTEN tumor suppressor, which dephosphorylates the lipids that mediate PI 3-kinase functions, whereas constitutively active Akt impaired insulin-promoted IRS-1 tyrosine phosphorylation. Conversely, TNF inhibition of IRS-1 tyrosine phosphorylation was blocked by kinase dead Akt. Inhibition of IRS-1 tyrosine phosphorylation by TNF was blocked by rapamycin, an inhibitor of the mammalian target of rapamycin (mTOR), a downstream target of Akt. mTOR induced the serine phosphorylation of IRS-1 (Ser-636/639), and such phosphorylation was inhibited by rapamycin. These results suggest that TNF impairs insulin signaling through IRS-1 by activation of a PI 3-kinase/Akt/mTOR pathway, which is antagonized by PTEN.

DOI: 10.1073/pnas.051042298
PubMed: 11287630
PubMed Central: PMC31887

Affiliations:

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<term>Cell Line (MeSH)</term>
<term>Chromatography, Liquid (MeSH)</term>
<term>Humans (MeSH)</term>
<term>Insulin (metabolism)</term>
<term>Insulin Receptor Substrate Proteins (MeSH)</term>
<term>Insulin Resistance (MeSH)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>PTEN Phosphohydrolase (MeSH)</term>
<term>Phosphatidylinositol 3-Kinases (metabolism)</term>
<term>Phosphoproteins (metabolism)</term>
<term>Phosphoric Monoester Hydrolases (metabolism)</term>
<term>Phosphorylation (MeSH)</term>
<term>Phosphotransferases (Alcohol Group Acceptor) (metabolism)</term>
<term>Protein Kinases (MeSH)</term>
<term>Protein-Serine-Threonine Kinases (MeSH)</term>
<term>Proto-Oncogene Proteins (metabolism)</term>
<term>Proto-Oncogene Proteins c-akt (MeSH)</term>
<term>Signal Transduction (MeSH)</term>
<term>Spectrometry, Mass, Electrospray Ionization (MeSH)</term>
<term>TOR Serine-Threonine Kinases (MeSH)</term>
<term>Tumor Necrosis Factor-alpha (antagonists & inhibitors)</term>
<term>Tumor Suppressor Proteins (MeSH)</term>
<term>Tyrosine (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Chromatographie en phase liquide (MeSH)</term>
<term>Données de séquences moléculaires (MeSH)</term>
<term>Facteur de nécrose tumorale alpha (antagonistes et inhibiteurs)</term>
<term>Humains (MeSH)</term>
<term>Insuline (métabolisme)</term>
<term>Insulinorésistance (MeSH)</term>
<term>Lignée cellulaire (MeSH)</term>
<term>Phosphatidylinositol 3-kinases (métabolisme)</term>
<term>Phosphohydrolase PTEN (MeSH)</term>
<term>Phosphoprotéines (métabolisme)</term>
<term>Phosphoric monoester hydrolases (métabolisme)</term>
<term>Phosphorylation (MeSH)</term>
<term>Phosphotransferases (Alcohol Group Acceptor) (métabolisme)</term>
<term>Protein kinases (MeSH)</term>
<term>Protein-Serine-Threonine Kinases (MeSH)</term>
<term>Protéines proto-oncogènes (métabolisme)</term>
<term>Protéines proto-oncogènes c-akt (MeSH)</term>
<term>Protéines suppresseurs de tumeurs (MeSH)</term>
<term>Spectrométrie de masse ESI (MeSH)</term>
<term>Substrats du récepteur à l'insuline (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
<term>Sérine-thréonine kinases TOR (MeSH)</term>
<term>Transduction du signal (MeSH)</term>
<term>Tyrosine (métabolisme)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Tumor Necrosis Factor-alpha</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Insulin</term>
<term>Phosphatidylinositol 3-Kinases</term>
<term>Phosphoproteins</term>
<term>Phosphoric Monoester Hydrolases</term>
<term>Phosphotransferases (Alcohol Group Acceptor)</term>
<term>Proto-Oncogene Proteins</term>
<term>Tyrosine</term>
</keywords>
<keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Facteur de nécrose tumorale alpha</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Insuline</term>
<term>Phosphatidylinositol 3-kinases</term>
<term>Phosphoprotéines</term>
<term>Phosphoric monoester hydrolases</term>
<term>Phosphotransferases (Alcohol Group Acceptor)</term>
<term>Protéines proto-oncogènes</term>
<term>Tyrosine</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Cell Line</term>
<term>Chromatography, Liquid</term>
<term>Humans</term>
<term>Insulin Receptor Substrate Proteins</term>
<term>Insulin Resistance</term>
<term>Molecular Sequence Data</term>
<term>PTEN Phosphohydrolase</term>
<term>Phosphorylation</term>
<term>Protein Kinases</term>
<term>Protein-Serine-Threonine Kinases</term>
<term>Proto-Oncogene Proteins c-akt</term>
<term>Signal Transduction</term>
<term>Spectrometry, Mass, Electrospray Ionization</term>
<term>TOR Serine-Threonine Kinases</term>
<term>Tumor Suppressor Proteins</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Chromatographie en phase liquide</term>
<term>Données de séquences moléculaires</term>
<term>Humains</term>
<term>Insulinorésistance</term>
<term>Lignée cellulaire</term>
<term>Phosphohydrolase PTEN</term>
<term>Phosphorylation</term>
<term>Protein kinases</term>
<term>Protein-Serine-Threonine Kinases</term>
<term>Protéines proto-oncogènes c-akt</term>
<term>Protéines suppresseurs de tumeurs</term>
<term>Spectrométrie de masse ESI</term>
<term>Substrats du récepteur à l'insuline</term>
<term>Séquence d'acides aminés</term>
<term>Sérine-thréonine kinases TOR</term>
<term>Transduction du signal</term>
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<front><div type="abstract" xml:lang="en">Tyrosine phosphorylation of insulin receptor substrate-1 (IRS-1) by the insulin receptor permits this docking protein to interact with signaling proteins that promote insulin action. Serine phosphorylation uncouples IRS-1 from the insulin receptor, thereby inhibiting its tyrosine phosphorylation and insulin signaling. For this reason, there is great interest in identifying serine/threonine kinases for which IRS-1 is a substrate. Tumor necrosis factor (TNF) inhibited insulin-promoted tyrosine phosphorylation of IRS-1 and activated the Akt/protein kinase B serine-threonine kinase, a downstream target for phosphatidylinositol 3-kinase (PI 3-kinase). The effect of TNF on insulin-promoted tyrosine phosphorylation of IRS-1 was blocked by inhibition of PI 3-kinase and the PTEN tumor suppressor, which dephosphorylates the lipids that mediate PI 3-kinase functions, whereas constitutively active Akt impaired insulin-promoted IRS-1 tyrosine phosphorylation. Conversely, TNF inhibition of IRS-1 tyrosine phosphorylation was blocked by kinase dead Akt. Inhibition of IRS-1 tyrosine phosphorylation by TNF was blocked by rapamycin, an inhibitor of the mammalian target of rapamycin (mTOR), a downstream target of Akt. mTOR induced the serine phosphorylation of IRS-1 (Ser-636/639), and such phosphorylation was inhibited by rapamycin. These results suggest that TNF impairs insulin signaling through IRS-1 by activation of a PI 3-kinase/Akt/mTOR pathway, which is antagonized by PTEN.</div>
</front>
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<Month>05</Month>
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<Title>Proceedings of the National Academy of Sciences of the United States of America</Title>
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<ArticleTitle>A phosphatidylinositol 3-kinase/Akt/mTOR pathway mediates and PTEN antagonizes tumor necrosis factor inhibition of insulin signaling through insulin receptor substrate-1.</ArticleTitle>
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<Abstract><AbstractText>Tyrosine phosphorylation of insulin receptor substrate-1 (IRS-1) by the insulin receptor permits this docking protein to interact with signaling proteins that promote insulin action. Serine phosphorylation uncouples IRS-1 from the insulin receptor, thereby inhibiting its tyrosine phosphorylation and insulin signaling. For this reason, there is great interest in identifying serine/threonine kinases for which IRS-1 is a substrate. Tumor necrosis factor (TNF) inhibited insulin-promoted tyrosine phosphorylation of IRS-1 and activated the Akt/protein kinase B serine-threonine kinase, a downstream target for phosphatidylinositol 3-kinase (PI 3-kinase). The effect of TNF on insulin-promoted tyrosine phosphorylation of IRS-1 was blocked by inhibition of PI 3-kinase and the PTEN tumor suppressor, which dephosphorylates the lipids that mediate PI 3-kinase functions, whereas constitutively active Akt impaired insulin-promoted IRS-1 tyrosine phosphorylation. Conversely, TNF inhibition of IRS-1 tyrosine phosphorylation was blocked by kinase dead Akt. Inhibition of IRS-1 tyrosine phosphorylation by TNF was blocked by rapamycin, an inhibitor of the mammalian target of rapamycin (mTOR), a downstream target of Akt. mTOR induced the serine phosphorylation of IRS-1 (Ser-636/639), and such phosphorylation was inhibited by rapamycin. These results suggest that TNF impairs insulin signaling through IRS-1 by activation of a PI 3-kinase/Akt/mTOR pathway, which is antagonized by PTEN.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Ozes</LastName>
<ForeName>O N</ForeName>
<Initials>ON</Initials>
<AffiliationInfo><Affiliation>Department of Microbiology and Immunology, Indiana University School of Medicine and the Walther Oncology Center, Indianapolis, IN 46202, USA.</Affiliation>
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<Author ValidYN="Y"><LastName>Akca</LastName>
<ForeName>H</ForeName>
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<Author ValidYN="Y"><LastName>Mayo</LastName>
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<Author ValidYN="Y"><LastName>Gustin</LastName>
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<Author ValidYN="Y"><LastName>Maehama</LastName>
<ForeName>T</ForeName>
<Initials>T</Initials>
</Author>
<Author ValidYN="Y"><LastName>Dixon</LastName>
<ForeName>J E</ForeName>
<Initials>JE</Initials>
</Author>
<Author ValidYN="Y"><LastName>Donner</LastName>
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</Author>
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<Language>eng</Language>
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<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
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</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D007328">Insulin</NameOfSubstance>
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<Chemical><RegistryNumber>EC 2.7.-</RegistryNumber>
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<Chemical><RegistryNumber>EC 2.7.1.-</RegistryNumber>
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<Chemical><RegistryNumber>EC 2.7.1.-</RegistryNumber>
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<Chemical><RegistryNumber>EC 2.7.1.1</RegistryNumber>
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<Chemical><RegistryNumber>EC 2.7.1.1</RegistryNumber>
<NameOfSubstance UI="D058570">TOR Serine-Threonine Kinases</NameOfSubstance>
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<Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber>
<NameOfSubstance UI="C494918">AKT1 protein, human</NameOfSubstance>
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<Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber>
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<Chemical><RegistryNumber>EC 3.1.3.2</RegistryNumber>
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<Chemical><RegistryNumber>EC 3.1.3.67</RegistryNumber>
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<MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName>
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<MeshHeading><DescriptorName UI="D051057" MajorTopicYN="N">Proto-Oncogene Proteins c-akt</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D015398" MajorTopicYN="Y">Signal Transduction</DescriptorName>
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<MeshHeading><DescriptorName UI="D021241" MajorTopicYN="N">Spectrometry, Mass, Electrospray Ionization</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D058570" MajorTopicYN="N">TOR Serine-Threonine Kinases</DescriptorName>
</MeshHeading>
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<QualifierName UI="Q000037" MajorTopicYN="Y">antagonists & inhibitors</QualifierName>
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<MeshHeading><DescriptorName UI="D025521" MajorTopicYN="Y">Tumor Suppressor Proteins</DescriptorName>
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<MeshHeading><DescriptorName UI="D014443" MajorTopicYN="N">Tyrosine</DescriptorName>
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A phosphatidylinositol 3-kinase/Akt/mTOR pathway mediates and PTEN antagonizes tumor necrosis factor inhibition of insulin signaling through insulin receptor substrate-1.

A phosphatidylinositol 3-kinase/Akt/mTOR pathway mediates and PTEN antagonizes tumor necrosis factor inhibition of insulin signaling through insulin receptor substrate-1.

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