Inactivation of mammalian target of rapamycin increases STAT1 nuclear content and transcriptional activity in alpha4- and protein phosphatase 2A-dependent fashion.
Identifieur interne : 001514 ( Main/Exploration ); précédent : 001513; suivant : 001515Inactivation of mammalian target of rapamycin increases STAT1 nuclear content and transcriptional activity in alpha4- and protein phosphatase 2A-dependent fashion.
Auteurs : Jill A. Fielhaber [Canada] ; Ying-Shan Han ; Jason Tan ; Shuo Xing ; Catherine M. Biggs ; Kwang-Bo Joung ; Arnold S. KristofSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2009.
Descripteurs français
- KwdFr :
- Apoptose (génétique), Apoptose (immunologie), Chaperons moléculaires (MeSH), Complexes multiprotéiques (génétique), Complexes multiprotéiques (immunologie), Complexes multiprotéiques (métabolisme), Facteur de transcription STAT-1 (génétique), Facteur de transcription STAT-1 (immunologie), Facteur de transcription STAT-1 (métabolisme), Humains (MeSH), Lignée cellulaire (MeSH), Noyau de la cellule (génétique), Noyau de la cellule (immunologie), Noyau de la cellule (métabolisme), Protein Phosphatase 2 (génétique), Protein Phosphatase 2 (immunologie), Protein Phosphatase 2 (métabolisme), Protein kinases (génétique), Protein kinases (immunologie), Protein kinases (métabolisme), Protéines adaptatrices de la transduction du signal (génétique), Protéines adaptatrices de la transduction du signal (métabolisme), Protéines de Saccharomyces cerevisiae (génétique), Protéines de Saccharomyces cerevisiae (métabolisme), Protéines et peptides de signalisation intracellulaire (MeSH), Protéines proto-oncogènes c-akt (génétique), Protéines proto-oncogènes c-akt (immunologie), Protéines proto-oncogènes c-akt (métabolisme), Ribosomal Protein S6 Kinases, 70-kDa (génétique), Ribosomal Protein S6 Kinases, 70-kDa (immunologie), Ribosomal Protein S6 Kinases, 70-kDa (métabolisme), Régulation de l'expression des gènes (génétique), Régulation de l'expression des gènes (immunologie), Saccharomyces cerevisiae (génétique), Saccharomyces cerevisiae (métabolisme), Sérine-thréonine kinases TOR (MeSH).
- MESH :
- génétique : Apoptose, Complexes multiprotéiques, Facteur de transcription STAT-1, Noyau de la cellule, Protein Phosphatase 2, Protein kinases, Protéines adaptatrices de la transduction du signal, Protéines de Saccharomyces cerevisiae, Protéines proto-oncogènes c-akt, Ribosomal Protein S6 Kinases, 70-kDa, Régulation de l'expression des gènes, Saccharomyces cerevisiae.
- immunologie : Apoptose, Complexes multiprotéiques, Facteur de transcription STAT-1, Noyau de la cellule, Protein Phosphatase 2, Protein kinases, Protéines proto-oncogènes c-akt, Ribosomal Protein S6 Kinases, 70-kDa, Régulation de l'expression des gènes.
- métabolisme : Complexes multiprotéiques, Facteur de transcription STAT-1, Noyau de la cellule, Protein Phosphatase 2, Protein kinases, Protéines adaptatrices de la transduction du signal, Protéines de Saccharomyces cerevisiae, Protéines proto-oncogènes c-akt, Ribosomal Protein S6 Kinases, 70-kDa, Saccharomyces cerevisiae.
- Chaperons moléculaires, Humains, Lignée cellulaire, Protéines et peptides de signalisation intracellulaire, Sérine-thréonine kinases TOR.
English descriptors
- KwdEn :
- Adaptor Proteins, Signal Transducing (genetics), Adaptor Proteins, Signal Transducing (metabolism), Apoptosis (genetics), Apoptosis (immunology), Cell Line (MeSH), Cell Nucleus (genetics), Cell Nucleus (immunology), Cell Nucleus (metabolism), Gene Expression Regulation (genetics), Gene Expression Regulation (immunology), Humans (MeSH), Intracellular Signaling Peptides and Proteins (MeSH), Molecular Chaperones (MeSH), Multiprotein Complexes (genetics), Multiprotein Complexes (immunology), Multiprotein Complexes (metabolism), Protein Kinases (genetics), Protein Kinases (immunology), Protein Kinases (metabolism), Protein Phosphatase 2 (genetics), Protein Phosphatase 2 (immunology), Protein Phosphatase 2 (metabolism), Proto-Oncogene Proteins c-akt (genetics), Proto-Oncogene Proteins c-akt (immunology), Proto-Oncogene Proteins c-akt (metabolism), Ribosomal Protein S6 Kinases, 70-kDa (genetics), Ribosomal Protein S6 Kinases, 70-kDa (immunology), Ribosomal Protein S6 Kinases, 70-kDa (metabolism), STAT1 Transcription Factor (genetics), STAT1 Transcription Factor (immunology), STAT1 Transcription Factor (metabolism), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism), TOR Serine-Threonine Kinases (MeSH).
- MESH :
- chemical , genetics : Adaptor Proteins, Signal Transducing, Multiprotein Complexes, Protein Kinases, Protein Phosphatase 2, Proto-Oncogene Proteins c-akt, Ribosomal Protein S6 Kinases, 70-kDa, STAT1 Transcription Factor, Saccharomyces cerevisiae Proteins.
- chemical , immunology : Multiprotein Complexes, Protein Kinases, Protein Phosphatase 2, Proto-Oncogene Proteins c-akt, Ribosomal Protein S6 Kinases, 70-kDa, STAT1 Transcription Factor.
- chemical , metabolism : Adaptor Proteins, Signal Transducing, Multiprotein Complexes, Protein Kinases, Protein Phosphatase 2, Proto-Oncogene Proteins c-akt, Ribosomal Protein S6 Kinases, 70-kDa, STAT1 Transcription Factor, Saccharomyces cerevisiae Proteins.
- genetics : Apoptosis, Cell Nucleus, Gene Expression Regulation, Saccharomyces cerevisiae.
- immunology : Apoptosis, Cell Nucleus, Gene Expression Regulation.
- metabolism : Cell Nucleus, Saccharomyces cerevisiae.
- Cell Line, Humans, Intracellular Signaling Peptides and Proteins, Molecular Chaperones, TOR Serine-Threonine Kinases.
Abstract
Target of rapamycin (TOR) is a highly conserved serine/threonine kinase that controls cell growth, primarily via regulation of protein synthesis. In Saccharomyces cerevisiae, TOR can also suppress the transcription of stress response genes by a mechanism involving Tap42, a serine/threonine phosphatase subunit, and the transcription factor Msn2. A physical association between mammalian TOR (mTOR) and the transcription factor signal transducer and activator of transcription-1 (STAT1) was recently identified in human cells, suggesting a similar role for mTOR in the transcription of interferon-gamma-stimulated genes. In the current study, we identified a macromolecular protein complex composed of mTOR, STAT1, the Tap42 homologue alpha4, and the protein phosphatase 2A catalytic subunit (PP2Ac). Inactivation of mTOR enhanced its association with STAT1 and increased STAT1 nuclear content in PP2Ac-dependent fashion. Depletion of alpha4, PP2A, or mTOR enhanced the induction of early (i.e. IRF-1) and late (i.e. caspase-1, hiNOS, and Fas) STAT1-dependent genes. The regulation of IRF-1 or caspase-1 by mTOR was independent of other known mTOR effectors p70 S6 kinase and Akt. These results describe a new role for mTOR and alpha4/PP2A in the control of STAT1 nuclear content, and the expression of interferon-gamma-sensitive genes involved in immunity and apoptosis.
DOI: 10.1074/jbc.M109.033530
PubMed: 19553685
PubMed Central: PMC2782027
Affiliations:
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(metabolism)</term><term>Protein Kinases (genetics)</term><term>Protein Kinases (immunology)</term><term>Protein Kinases (metabolism)</term><term>Protein Phosphatase 2 (genetics)</term><term>Protein Phosphatase 2 (immunology)</term><term>Protein Phosphatase 2 (metabolism)</term><term>Proto-Oncogene Proteins c-akt (genetics)</term><term>Proto-Oncogene Proteins c-akt (immunology)</term><term>Proto-Oncogene Proteins c-akt (metabolism)</term><term>Ribosomal Protein S6 Kinases, 70-kDa (genetics)</term><term>Ribosomal Protein S6 Kinases, 70-kDa (immunology)</term><term>Ribosomal Protein S6 Kinases, 70-kDa (metabolism)</term><term>STAT1 Transcription Factor (genetics)</term><term>STAT1 Transcription Factor (immunology)</term><term>STAT1 Transcription Factor (metabolism)</term><term>Saccharomyces cerevisiae (genetics)</term><term>Saccharomyces cerevisiae (metabolism)</term><term>Saccharomyces cerevisiae Proteins (genetics)</term><term>Saccharomyces cerevisiae Proteins (metabolism)</term><term>TOR Serine-Threonine Kinases (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Apoptose (génétique)</term><term>Apoptose (immunologie)</term><term>Chaperons moléculaires (MeSH)</term><term>Complexes multiprotéiques (génétique)</term><term>Complexes multiprotéiques (immunologie)</term><term>Complexes multiprotéiques (métabolisme)</term><term>Facteur de transcription STAT-1 (génétique)</term><term>Facteur de transcription STAT-1 (immunologie)</term><term>Facteur de transcription STAT-1 (métabolisme)</term><term>Humains (MeSH)</term><term>Lignée cellulaire (MeSH)</term><term>Noyau de la cellule (génétique)</term><term>Noyau de la cellule (immunologie)</term><term>Noyau de la cellule (métabolisme)</term><term>Protein Phosphatase 2 (génétique)</term><term>Protein Phosphatase 2 (immunologie)</term><term>Protein Phosphatase 2 (métabolisme)</term><term>Protein kinases (génétique)</term><term>Protein kinases (immunologie)</term><term>Protein kinases (métabolisme)</term><term>Protéines adaptatrices de la transduction du signal (génétique)</term><term>Protéines adaptatrices de la transduction du signal (métabolisme)</term><term>Protéines de Saccharomyces cerevisiae (génétique)</term><term>Protéines de Saccharomyces cerevisiae (métabolisme)</term><term>Protéines et peptides de signalisation intracellulaire (MeSH)</term><term>Protéines proto-oncogènes c-akt (génétique)</term><term>Protéines proto-oncogènes c-akt (immunologie)</term><term>Protéines proto-oncogènes c-akt (métabolisme)</term><term>Ribosomal Protein S6 Kinases, 70-kDa (génétique)</term><term>Ribosomal Protein S6 Kinases, 70-kDa (immunologie)</term><term>Ribosomal Protein S6 Kinases, 70-kDa (métabolisme)</term><term>Régulation de l'expression des gènes (génétique)</term><term>Régulation de l'expression des gènes (immunologie)</term><term>Saccharomyces cerevisiae (génétique)</term><term>Saccharomyces cerevisiae (métabolisme)</term><term>Sérine-thréonine kinases TOR (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Adaptor Proteins, Signal Transducing</term><term>Multiprotein Complexes</term><term>Protein Kinases</term><term>Protein Phosphatase 2</term><term>Proto-Oncogene Proteins c-akt</term><term>Ribosomal Protein S6 Kinases, 70-kDa</term><term>STAT1 Transcription Factor</term><term>Saccharomyces cerevisiae Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Multiprotein Complexes</term><term>Protein Kinases</term><term>Protein Phosphatase 2</term><term>Proto-Oncogene Proteins c-akt</term><term>Ribosomal Protein S6 Kinases, 70-kDa</term><term>STAT1 Transcription Factor</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Adaptor Proteins, Signal Transducing</term><term>Multiprotein Complexes</term><term>Protein Kinases</term><term>Protein Phosphatase 2</term><term>Proto-Oncogene Proteins c-akt</term><term>Ribosomal Protein S6 Kinases, 70-kDa</term><term>STAT1 Transcription Factor</term><term>Saccharomyces cerevisiae Proteins</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Apoptosis</term><term>Cell Nucleus</term><term>Gene Expression Regulation</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Apoptose</term><term>Complexes multiprotéiques</term><term>Facteur de transcription STAT-1</term><term>Noyau de la cellule</term><term>Protein Phosphatase 2</term><term>Protein kinases</term><term>Protéines adaptatrices de la transduction du signal</term><term>Protéines de Saccharomyces cerevisiae</term><term>Protéines proto-oncogènes c-akt</term><term>Ribosomal Protein S6 Kinases, 70-kDa</term><term>Régulation de l'expression des gènes</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Apoptose</term><term>Complexes multiprotéiques</term><term>Facteur de transcription STAT-1</term><term>Noyau de la cellule</term><term>Protein Phosphatase 2</term><term>Protein kinases</term><term>Protéines proto-oncogènes c-akt</term><term>Ribosomal Protein S6 Kinases, 70-kDa</term><term>Régulation de l'expression des gènes</term></keywords><keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Apoptosis</term><term>Cell Nucleus</term><term>Gene Expression Regulation</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cell Nucleus</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Complexes multiprotéiques</term><term>Facteur de transcription STAT-1</term><term>Noyau de la cellule</term><term>Protein Phosphatase 2</term><term>Protein kinases</term><term>Protéines adaptatrices de la transduction du signal</term><term>Protéines de Saccharomyces cerevisiae</term><term>Protéines proto-oncogènes c-akt</term><term>Ribosomal Protein S6 Kinases, 70-kDa</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cell Line</term><term>Humans</term><term>Intracellular Signaling Peptides and Proteins</term><term>Molecular Chaperones</term><term>TOR Serine-Threonine Kinases</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Chaperons moléculaires</term><term>Humains</term><term>Lignée cellulaire</term><term>Protéines et peptides de signalisation intracellulaire</term><term>Sérine-thréonine kinases TOR</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Target of rapamycin (TOR) is a highly conserved serine/threonine kinase that controls cell growth, primarily via regulation of protein synthesis. In Saccharomyces cerevisiae, TOR can also suppress the transcription of stress response genes by a mechanism involving Tap42, a serine/threonine phosphatase subunit, and the transcription factor Msn2. A physical association between mammalian TOR (mTOR) and the transcription factor signal transducer and activator of transcription-1 (STAT1) was recently identified in human cells, suggesting a similar role for mTOR in the transcription of interferon-gamma-stimulated genes. In the current study, we identified a macromolecular protein complex composed of mTOR, STAT1, the Tap42 homologue alpha4, and the protein phosphatase 2A catalytic subunit (PP2Ac). Inactivation of mTOR enhanced its association with STAT1 and increased STAT1 nuclear content in PP2Ac-dependent fashion. Depletion of alpha4, PP2A, or mTOR enhanced the induction of early (i.e. IRF-1) and late (i.e. caspase-1, hiNOS, and Fas) STAT1-dependent genes. The regulation of IRF-1 or caspase-1 by mTOR was independent of other known mTOR effectors p70 S6 kinase and Akt. These results describe a new role for mTOR and alpha4/PP2A in the control of STAT1 nuclear content, and the expression of interferon-gamma-sensitive genes involved in immunity and apoptosis.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">19553685</PMID><DateCompleted><Year>2009</Year><Month>10</Month><Day>05</Day></DateCompleted><DateRevised><Year>2019</Year><Month>12</Month><Day>10</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>284</Volume><Issue>36</Issue><PubDate><Year>2009</Year><Month>Sep</Month><Day>04</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Inactivation of mammalian target of rapamycin increases STAT1 nuclear content and transcriptional activity in alpha4- and protein phosphatase 2A-dependent fashion.</ArticleTitle><Pagination><MedlinePgn>24341-53</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1074/jbc.M109.033530</ELocationID><Abstract><AbstractText>Target of rapamycin (TOR) is a highly conserved serine/threonine kinase that controls cell growth, primarily via regulation of protein synthesis. In Saccharomyces cerevisiae, TOR can also suppress the transcription of stress response genes by a mechanism involving Tap42, a serine/threonine phosphatase subunit, and the transcription factor Msn2. A physical association between mammalian TOR (mTOR) and the transcription factor signal transducer and activator of transcription-1 (STAT1) was recently identified in human cells, suggesting a similar role for mTOR in the transcription of interferon-gamma-stimulated genes. In the current study, we identified a macromolecular protein complex composed of mTOR, STAT1, the Tap42 homologue alpha4, and the protein phosphatase 2A catalytic subunit (PP2Ac). Inactivation of mTOR enhanced its association with STAT1 and increased STAT1 nuclear content in PP2Ac-dependent fashion. Depletion of alpha4, PP2A, or mTOR enhanced the induction of early (i.e. IRF-1) and late (i.e. caspase-1, hiNOS, and Fas) STAT1-dependent genes. The regulation of IRF-1 or caspase-1 by mTOR was independent of other known mTOR effectors p70 S6 kinase and Akt. These results describe a new role for mTOR and alpha4/PP2A in the control of STAT1 nuclear content, and the expression of interferon-gamma-sensitive genes involved in immunity and apoptosis.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Fielhaber</LastName><ForeName>Jill A</ForeName><Initials>JA</Initials><AffiliationInfo><Affiliation>Critical Care and Respiratory Divisions and Meakins-Christie Laboratories, Faculty of Medicine, McGill University, Montreal, Quebec H3A 1A1, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Han</LastName><ForeName>Ying-Shan</ForeName><Initials>YS</Initials></Author><Author ValidYN="Y"><LastName>Tan</LastName><ForeName>Jason</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Xing</LastName><ForeName>Shuo</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Biggs</LastName><ForeName>Catherine M</ForeName><Initials>CM</Initials></Author><Author ValidYN="Y"><LastName>Joung</LastName><ForeName>Kwang-Bo</ForeName><Initials>KB</Initials></Author><Author ValidYN="Y"><LastName>Kristof</LastName><ForeName>Arnold S</ForeName><Initials>AS</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01 CA125436-01A1</GrantID><Acronym>CA</Acronym><Agency>NCI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>5R01CA125436</GrantID><Acronym>CA</Acronym><Agency>NCI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 CA125436-02</GrantID><Acronym>CA</Acronym><Agency>NCI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 CA125436-03</GrantID><Acronym>CA</Acronym><Agency>NCI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>69007</GrantID><Agency>Canadian Institutes of Health Research</Agency><Country>Canada</Country></Grant><Grant><GrantID>R01 CA125436</GrantID><Acronym>CA</Acronym><Agency>NCI 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><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2009</Year><Month>06</Month><Day>24</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Biol Chem</MedlineTA><NlmUniqueID>2985121R</NlmUniqueID><ISSNLinking>0021-9258</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D048868">Adaptor Proteins, Signal Transducing</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C490467">IGBP1 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D047908">Intracellular Signaling Peptides 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Biggs</name><name sortKey="Han, Ying Shan" sort="Han, Ying Shan" uniqKey="Han Y" first="Ying-Shan" last="Han">Ying-Shan Han</name><name sortKey="Joung, Kwang Bo" sort="Joung, Kwang Bo" uniqKey="Joung K" first="Kwang-Bo" last="Joung">Kwang-Bo Joung</name><name sortKey="Kristof, Arnold S" sort="Kristof, Arnold S" uniqKey="Kristof A" first="Arnold S" last="Kristof">Arnold S. Kristof</name><name sortKey="Tan, Jason" sort="Tan, Jason" uniqKey="Tan J" first="Jason" last="Tan">Jason Tan</name><name sortKey="Xing, Shuo" sort="Xing, Shuo" uniqKey="Xing S" first="Shuo" last="Xing">Shuo Xing</name></noCountry><country name="Canada"><region name="Québec"><name sortKey="Fielhaber, Jill A" sort="Fielhaber, Jill A" uniqKey="Fielhaber J" first="Jill A" last="Fielhaber">Jill A. Fielhaber</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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