Regulation of TAK1/TAB1-mediated IL-1β signaling by cytoplasmic PPARβ/δ
The peroxisome proliferator-activated receptor subtypes PPARα, PPARβ/δ, PPARγ are members of the steroid hormone receptor superfamily with well-established functions in transcriptional regulation. Here, we describe an unexpected cytoplasmic function of PPARβ/δ. Silencing of PPARβ/δ expression interf...
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| Veröffentlicht in: | PloS one 2013-04, Vol.8 (4), p.e63011 |
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| creator | Stockert, Josefine Wolf, Alexander Kaddatz, Kerstin Schnitzer, Evelyn Finkernagel, Florian Meissner, Wolfgang Müller-Brüsselbach, Sabine Kracht, Michael Müller, Rolf |
| description | The peroxisome proliferator-activated receptor subtypes PPARα, PPARβ/δ, PPARγ are members of the steroid hormone receptor superfamily with well-established functions in transcriptional regulation. Here, we describe an unexpected cytoplasmic function of PPARβ/δ. Silencing of PPARβ/δ expression interferes with the expression of a large subset of interleukin-1β (IL-1β)-induced target genes in HeLa cells, which is preceded by an inhibition of the IL-1β-induced phosphorylation of TAK1 and its downstream effectors, including the NFκBα inhibitor IκBα (NFKBIA) and the NFκBα subunit p65 (RELA). PPARβ/δ enhances the interaction between TAK1 and the small heat-shock protein HSP27, a known positive modulator of TAK1-mediated IL-1β signaling. Consistent with these findings, PPARβ/δ physically interacts with both the endogenous cytoplasmic TAK1/TAB1 complex and HSP27, and PPARβ/δ overexpression increases the TAK1-induced transcriptional activity of NFκB. These observations suggest that PPARβ/δ plays a role in the assembly of a cytoplasmic multi-protein complex containing TAK1, TAB1, HSP27 and PPARβ/δ, and thereby participates in the NFκB response to IL-1β. |
| doi_str_mv | 10.1371/journal.pone.0063011 |
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Here, we describe an unexpected cytoplasmic function of PPARβ/δ. Silencing of PPARβ/δ expression interferes with the expression of a large subset of interleukin-1β (IL-1β)-induced target genes in HeLa cells, which is preceded by an inhibition of the IL-1β-induced phosphorylation of TAK1 and its downstream effectors, including the NFκBα inhibitor IκBα (NFKBIA) and the NFκBα subunit p65 (RELA). PPARβ/δ enhances the interaction between TAK1 and the small heat-shock protein HSP27, a known positive modulator of TAK1-mediated IL-1β signaling. Consistent with these findings, PPARβ/δ physically interacts with both the endogenous cytoplasmic TAK1/TAB1 complex and HSP27, and PPARβ/δ overexpression increases the TAK1-induced transcriptional activity of NFκB. These observations suggest that PPARβ/δ plays a role in the assembly of a cytoplasmic multi-protein complex containing TAK1, TAB1, HSP27 and PPARβ/δ, and thereby participates in the NFκB response to IL-1β.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0063011</identifier><identifier>PMID: 23646170</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Adaptor Proteins, Signal Transducing - metabolism ; Apoptosis ; Biology ; Cancer ; Cytokines ; Cytoplasm - metabolism ; Fatty acids ; Gene expression ; Gene Expression Profiling ; Gene Expression Regulation ; Gene regulation ; Genomes ; Growth factors ; Heat shock proteins ; HeLa Cells ; HSP27 Heat-Shock Proteins - metabolism ; Hsp27 protein ; Humans ; IL-1β ; Inflammation ; Interleukin-1beta - metabolism ; Interleukin-1beta - pharmacology ; Interleukins ; Kinases ; Ligands ; MAP Kinase Kinase Kinases - chemistry ; MAP Kinase Kinase Kinases - metabolism ; Metabolism ; Metabolites ; Molecular biology ; Musculoskeletal system ; NF-κB protein ; Phosphorylation ; PPAR delta - metabolism ; PPAR-beta - metabolism ; Protein Binding ; Protein Interaction Domains and Motifs ; RelA protein ; Rodents ; Signal Transduction ; Signaling ; Skin ; TAK1 protein ; Transcription ; Transcription Factor RelA - metabolism ; Transcription factors ; Transcription, Genetic - drug effects</subject><ispartof>PloS one, 2013-04, Vol.8 (4), p.e63011</ispartof><rights>2013 Stockert et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: https://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2013 Stockert et al 2013 Stockert et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c526t-cd2f26125b3c0f5e445159676003e2fe8710b5ff51562268b1858fdf02cb4b13</citedby><cites>FETCH-LOGICAL-c526t-cd2f26125b3c0f5e445159676003e2fe8710b5ff51562268b1858fdf02cb4b13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3639976/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3639976/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,2096,2915,23845,27901,27902,53766,53768,79342,79343</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23646170$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Stockert, Josefine</creatorcontrib><creatorcontrib>Wolf, Alexander</creatorcontrib><creatorcontrib>Kaddatz, Kerstin</creatorcontrib><creatorcontrib>Schnitzer, Evelyn</creatorcontrib><creatorcontrib>Finkernagel, Florian</creatorcontrib><creatorcontrib>Meissner, Wolfgang</creatorcontrib><creatorcontrib>Müller-Brüsselbach, Sabine</creatorcontrib><creatorcontrib>Kracht, Michael</creatorcontrib><creatorcontrib>Müller, Rolf</creatorcontrib><title>Regulation of TAK1/TAB1-mediated IL-1β signaling by cytoplasmic PPARβ/δ</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>The peroxisome proliferator-activated receptor subtypes PPARα, PPARβ/δ, PPARγ are members of the steroid hormone receptor superfamily with well-established functions in transcriptional regulation. Here, we describe an unexpected cytoplasmic function of PPARβ/δ. Silencing of PPARβ/δ expression interferes with the expression of a large subset of interleukin-1β (IL-1β)-induced target genes in HeLa cells, which is preceded by an inhibition of the IL-1β-induced phosphorylation of TAK1 and its downstream effectors, including the NFκBα inhibitor IκBα (NFKBIA) and the NFκBα subunit p65 (RELA). PPARβ/δ enhances the interaction between TAK1 and the small heat-shock protein HSP27, a known positive modulator of TAK1-mediated IL-1β signaling. Consistent with these findings, PPARβ/δ physically interacts with both the endogenous cytoplasmic TAK1/TAB1 complex and HSP27, and PPARβ/δ overexpression increases the TAK1-induced transcriptional activity of NFκB. These observations suggest that PPARβ/δ plays a role in the assembly of a cytoplasmic multi-protein complex containing TAK1, TAB1, HSP27 and PPARβ/δ, and thereby participates in the NFκB response to IL-1β.</description><subject>Adaptor Proteins, Signal Transducing - metabolism</subject><subject>Apoptosis</subject><subject>Biology</subject><subject>Cancer</subject><subject>Cytokines</subject><subject>Cytoplasm - metabolism</subject><subject>Fatty acids</subject><subject>Gene expression</subject><subject>Gene Expression Profiling</subject><subject>Gene Expression Regulation</subject><subject>Gene regulation</subject><subject>Genomes</subject><subject>Growth factors</subject><subject>Heat shock proteins</subject><subject>HeLa Cells</subject><subject>HSP27 Heat-Shock Proteins - metabolism</subject><subject>Hsp27 protein</subject><subject>Humans</subject><subject>IL-1β</subject><subject>Inflammation</subject><subject>Interleukin-1beta - metabolism</subject><subject>Interleukin-1beta - pharmacology</subject><subject>Interleukins</subject><subject>Kinases</subject><subject>Ligands</subject><subject>MAP Kinase Kinase Kinases - chemistry</subject><subject>MAP Kinase Kinase Kinases - metabolism</subject><subject>Metabolism</subject><subject>Metabolites</subject><subject>Molecular biology</subject><subject>Musculoskeletal system</subject><subject>NF-κB protein</subject><subject>Phosphorylation</subject><subject>PPAR delta - metabolism</subject><subject>PPAR-beta - metabolism</subject><subject>Protein Binding</subject><subject>Protein Interaction Domains and Motifs</subject><subject>RelA protein</subject><subject>Rodents</subject><subject>Signal Transduction</subject><subject>Signaling</subject><subject>Skin</subject><subject>TAK1 protein</subject><subject>Transcription</subject><subject>Transcription Factor RelA - metabolism</subject><subject>Transcription factors</subject><subject>Transcription, Genetic - drug effects</subject><issn>1932-6203</issn><issn>1932-6203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><sourceid>DOA</sourceid><recordid>eNp1Ud1q2zAUFmNj_dsbjNWwayc6kiXbN4W09CdroKXkXkiy5Ck4ViY5g7xW6XPkmeo0bmkveiVxzvdz-D6EfgIeAc1hvPDr0MpmtPKtGWHMKQb4gg6hpCTlBNOv7_4H6CjGBcaMFpx_RweE8oxDjg_RnwdTrxvZOd8m3ibzyS2M55NzSJemcrIzVTKdpbB9TKKrezfX1onaJHrT-VUj49Lp5P5-8rB9HG-fTtA3K5tofgzvMZpfXc4vbtLZ3fX0YjJLNSO8S3VFLOFAmKIaW2ayjAErec4xpoZYU-SAFbO2n3JCeKGgYIWtLCZaZQroMTrdy64aH8WQQhRAswIIKdgOMd0jKi8XYhXcUoaN8NKJl4EPtZChc7oxgvfuvZ_Z5ZdllhS8pKCIUqCNlabstc4Gt7XqI9Gm7YJsPoh-3LTur6j9f0E5Lcuc9wK_B4Hg_61N7D45OdujdPAxBmPfHACLXd2vLLGrWwx197Rf7697I732S58BDW2ntw</recordid><startdate>20130430</startdate><enddate>20130430</enddate><creator>Stockert, Josefine</creator><creator>Wolf, Alexander</creator><creator>Kaddatz, Kerstin</creator><creator>Schnitzer, Evelyn</creator><creator>Finkernagel, Florian</creator><creator>Meissner, Wolfgang</creator><creator>Müller-Brüsselbach, Sabine</creator><creator>Kracht, Michael</creator><creator>Müller, Rolf</creator><general>Public Library of Science</general><general>Public Library of Science (PLoS)</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QO</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TG</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PDBOC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>RC3</scope><scope>5PM</scope><scope>DOA</scope></search><sort><creationdate>20130430</creationdate><title>Regulation of TAK1/TAB1-mediated IL-1β signaling by cytoplasmic PPARβ/δ</title><author>Stockert, Josefine ; Wolf, Alexander ; Kaddatz, Kerstin ; Schnitzer, Evelyn ; Finkernagel, Florian ; Meissner, Wolfgang ; Müller-Brüsselbach, Sabine ; Kracht, Michael ; Müller, Rolf</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c526t-cd2f26125b3c0f5e445159676003e2fe8710b5ff51562268b1858fdf02cb4b13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Adaptor Proteins, Signal Transducing - metabolism</topic><topic>Apoptosis</topic><topic>Biology</topic><topic>Cancer</topic><topic>Cytokines</topic><topic>Cytoplasm - metabolism</topic><topic>Fatty acids</topic><topic>Gene expression</topic><topic>Gene Expression Profiling</topic><topic>Gene Expression Regulation</topic><topic>Gene regulation</topic><topic>Genomes</topic><topic>Growth factors</topic><topic>Heat shock proteins</topic><topic>HeLa Cells</topic><topic>HSP27 Heat-Shock Proteins - metabolism</topic><topic>Hsp27 protein</topic><topic>Humans</topic><topic>IL-1β</topic><topic>Inflammation</topic><topic>Interleukin-1beta - metabolism</topic><topic>Interleukin-1beta - pharmacology</topic><topic>Interleukins</topic><topic>Kinases</topic><topic>Ligands</topic><topic>MAP Kinase Kinase Kinases - chemistry</topic><topic>MAP Kinase Kinase Kinases - metabolism</topic><topic>Metabolism</topic><topic>Metabolites</topic><topic>Molecular biology</topic><topic>Musculoskeletal system</topic><topic>NF-κB protein</topic><topic>Phosphorylation</topic><topic>PPAR delta - metabolism</topic><topic>PPAR-beta - metabolism</topic><topic>Protein Binding</topic><topic>Protein Interaction Domains and Motifs</topic><topic>RelA protein</topic><topic>Rodents</topic><topic>Signal Transduction</topic><topic>Signaling</topic><topic>Skin</topic><topic>TAK1 protein</topic><topic>Transcription</topic><topic>Transcription Factor RelA - metabolism</topic><topic>Transcription factors</topic><topic>Transcription, Genetic - drug effects</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Stockert, Josefine</creatorcontrib><creatorcontrib>Wolf, Alexander</creatorcontrib><creatorcontrib>Kaddatz, Kerstin</creatorcontrib><creatorcontrib>Schnitzer, Evelyn</creatorcontrib><creatorcontrib>Finkernagel, Florian</creatorcontrib><creatorcontrib>Meissner, Wolfgang</creatorcontrib><creatorcontrib>Müller-Brüsselbach, Sabine</creatorcontrib><creatorcontrib>Kracht, Michael</creatorcontrib><creatorcontrib>Müller, Rolf</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Nursing & Allied Health Database</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Meteorological & Geoastrophysical Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Agricultural Science Collection</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>Advanced Technologies & Aerospace Collection</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Materials Science Database</collection><collection>Nursing & Allied Health Database (Alumni Edition)</collection><collection>Meteorological & Geoastrophysical Abstracts - 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Here, we describe an unexpected cytoplasmic function of PPARβ/δ. Silencing of PPARβ/δ expression interferes with the expression of a large subset of interleukin-1β (IL-1β)-induced target genes in HeLa cells, which is preceded by an inhibition of the IL-1β-induced phosphorylation of TAK1 and its downstream effectors, including the NFκBα inhibitor IκBα (NFKBIA) and the NFκBα subunit p65 (RELA). PPARβ/δ enhances the interaction between TAK1 and the small heat-shock protein HSP27, a known positive modulator of TAK1-mediated IL-1β signaling. Consistent with these findings, PPARβ/δ physically interacts with both the endogenous cytoplasmic TAK1/TAB1 complex and HSP27, and PPARβ/δ overexpression increases the TAK1-induced transcriptional activity of NFκB. These observations suggest that PPARβ/δ plays a role in the assembly of a cytoplasmic multi-protein complex containing TAK1, TAB1, HSP27 and PPARβ/δ, and thereby participates in the NFκB response to IL-1β.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>23646170</pmid><doi>10.1371/journal.pone.0063011</doi><oa>free_for_read</oa></addata></record> |
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| subjects | Adaptor Proteins, Signal Transducing - metabolism Apoptosis Biology Cancer Cytokines Cytoplasm - metabolism Fatty acids Gene expression Gene Expression Profiling Gene Expression Regulation Gene regulation Genomes Growth factors Heat shock proteins HeLa Cells HSP27 Heat-Shock Proteins - metabolism Hsp27 protein Humans IL-1β Inflammation Interleukin-1beta - metabolism Interleukin-1beta - pharmacology Interleukins Kinases Ligands MAP Kinase Kinase Kinases - chemistry MAP Kinase Kinase Kinases - metabolism Metabolism Metabolites Molecular biology Musculoskeletal system NF-κB protein Phosphorylation PPAR delta - metabolism PPAR-beta - metabolism Protein Binding Protein Interaction Domains and Motifs RelA protein Rodents Signal Transduction Signaling Skin TAK1 protein Transcription Transcription Factor RelA - metabolism Transcription factors Transcription, Genetic - drug effects |
| title | Regulation of TAK1/TAB1-mediated IL-1β signaling by cytoplasmic PPARβ/δ |
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