The TRAP/Mediator Coactivator Complex Interacts Directly with Estrogen Receptors α and β through the TRAP220 Subunit and Directly Enhances Estrogen Receptor Function in vitro
Target gene activation by nuclear hormone receptors, including estrogen receptors (ERs), is thought to be mediated by a variety of interacting cofactors. Here we identify a number of nuclear extract-derived proteins that interact with immobilized ER ligand binding domains in a 17β-estradiol-dependen...
Gespeichert in:
| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2002-03, Vol.99 (5), p.2642-2647 |
|---|---|
| Hauptverfasser: | , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 2647 |
|---|---|
| container_issue | 5 |
| container_start_page | 2642 |
| container_title | Proceedings of the National Academy of Sciences - PNAS |
| container_volume | 99 |
| creator | Kang, Yun Kyoung Guermah, Mohamed Yuan, Chao-Xing Roeder, Robert G. |
| description | Target gene activation by nuclear hormone receptors, including estrogen receptors (ERs), is thought to be mediated by a variety of interacting cofactors. Here we identify a number of nuclear extract-derived proteins that interact with immobilized ER ligand binding domains in a 17β-estradiol-dependent manner. The most prominent of these are components of the thyroid hormone receptor-associated protein (TRAP)/Mediator coactivator complex, which interacts with ERα and ERβ in both unfractionated nuclear extracts and purified form. Studies with extracts from TRAP220-/-fibroblasts reveal that these interactions depend on TRAP220, a TRAP/Mediator subunit previously shown to interact with ER and other nuclear receptors in a ligand-dependent manner. The physiological relevance of the in vitro interaction is documented further by the isolation of an ERα-TRAP/Mediator complex from cultured cells expressing an epitope-tagged ERα. Finally, the complete TRAP/Mediator complex is shown to enhance ER function directly in a highly purified cell-free transcription system. These studies firmly establish a direct role for TRAP/Mediator, through TRAP220, in ER function. |
| doi_str_mv | 10.1073/pnas.261715899 |
| format | Article |
| fullrecord | <record><control><sourceid>jstor_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_122401</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><jstor_id>3058002</jstor_id><sourcerecordid>3058002</sourcerecordid><originalsourceid>FETCH-LOGICAL-c464t-7dd6af70a80a975a2ac2707fe805ede0565a73973fd5556850d5c211e5148c443</originalsourceid><addsrcrecordid>eNqFks9uEzEQxlcIREPhygkhiwO3Tcdee-09cKhCCpWKQCWcLdfrzTra2KntDfStgAfpM-GSKPw7cBrL8_tmxp6vKJ5imGLg1cnGqTglNeaYiaa5V0wwNLisaQP3iwkA4aWghB4Vj2JcAUDDBDwsjjAWNed1Mym-LnqDFpenH07emdaq5AOaeaWT3e7P681gvqBzl0zI1xG9tsHoNNygzzb1aB5T8Evj0KXRZpMVEd1-Q8q16PY7Sn3w47LPcdeCEEAfx6vR2fQTOZSau145beK_5dDZ6PIw3iHr0Nbm7OPiQaeGaJ7s43Hx6Wy-mL0tL96_OZ-dXpSa1jSVvG1r1XFQAlTDmSJKEw68MwKYaQ2wmileNbzqWsZYLRi0TBOMDcNUaEqr4-LVru5mvFqbVhuXghrkJti1CjfSKyv_zDjby6XfSkwIBZz1L_f64K9HE5Nc26jNMChn_BhlXlglaqD_BbEgnBJeZfDFX-DKj8HlT5AkN2wYxZCh6Q7SwccYTHeYGIO8c4y8c4w8OCYLnv_-zl_43iIZeLYDVjEv5JCvIFsJSPUD6e_J8Q</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>201395410</pqid></control><display><type>article</type><title>The TRAP/Mediator Coactivator Complex Interacts Directly with Estrogen Receptors α and β through the TRAP220 Subunit and Directly Enhances Estrogen Receptor Function in vitro</title><source>MEDLINE</source><source>Full-Text Journals in Chemistry (Open access)</source><source>PubMed Central</source><source>Alma/SFX Local Collection</source><source>JSTOR</source><creator>Kang, Yun Kyoung ; Guermah, Mohamed ; Yuan, Chao-Xing ; Roeder, Robert G.</creator><creatorcontrib>Kang, Yun Kyoung ; Guermah, Mohamed ; Yuan, Chao-Xing ; Roeder, Robert G.</creatorcontrib><description>Target gene activation by nuclear hormone receptors, including estrogen receptors (ERs), is thought to be mediated by a variety of interacting cofactors. Here we identify a number of nuclear extract-derived proteins that interact with immobilized ER ligand binding domains in a 17β-estradiol-dependent manner. The most prominent of these are components of the thyroid hormone receptor-associated protein (TRAP)/Mediator coactivator complex, which interacts with ERα and ERβ in both unfractionated nuclear extracts and purified form. Studies with extracts from TRAP220-/-fibroblasts reveal that these interactions depend on TRAP220, a TRAP/Mediator subunit previously shown to interact with ER and other nuclear receptors in a ligand-dependent manner. The physiological relevance of the in vitro interaction is documented further by the isolation of an ERα-TRAP/Mediator complex from cultured cells expressing an epitope-tagged ERα. Finally, the complete TRAP/Mediator complex is shown to enhance ER function directly in a highly purified cell-free transcription system. These studies firmly establish a direct role for TRAP/Mediator, through TRAP220, in ER function.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.261715899</identifier><identifier>PMID: 11867769</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Animals ; Antibodies ; Biochemistry ; Biological Sciences ; Carrier Proteins - metabolism ; Cell Extracts ; Cell Line, Transformed ; Cell lines ; Cell Nucleus - metabolism ; Drug interactions ; Estradiol - pharmacology ; Estrogen Receptor alpha ; Estrogen Receptor beta ; Estrogens ; Genes ; HeLa Cells ; Hormones ; Humans ; Intracellular Fluid ; Ligands ; Mathematical functions ; Mediator complex ; Mediator Complex Subunit 1 ; Mice ; Nuclear interactions ; Nuclear receptors ; Proteins ; Receptors ; Receptors, Estrogen - genetics ; Receptors, Estrogen - metabolism ; Receptors, Thyroid Hormone - metabolism ; Recombinant Fusion Proteins - genetics ; Recombinant Fusion Proteins - metabolism ; Trans-Activators - metabolism ; Transcription Factors ; TRAP protein ; TRAP220 gene</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2002-03, Vol.99 (5), p.2642-2647</ispartof><rights>Copyright 1993-2002 National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences Mar 5, 2002</rights><rights>Copyright © 2002, The National Academy of Sciences 2002</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c464t-7dd6af70a80a975a2ac2707fe805ede0565a73973fd5556850d5c211e5148c443</citedby><cites>FETCH-LOGICAL-c464t-7dd6af70a80a975a2ac2707fe805ede0565a73973fd5556850d5c211e5148c443</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/3058002$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/3058002$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27901,27902,53766,53768,57992,58225</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11867769$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kang, Yun Kyoung</creatorcontrib><creatorcontrib>Guermah, Mohamed</creatorcontrib><creatorcontrib>Yuan, Chao-Xing</creatorcontrib><creatorcontrib>Roeder, Robert G.</creatorcontrib><title>The TRAP/Mediator Coactivator Complex Interacts Directly with Estrogen Receptors α and β through the TRAP220 Subunit and Directly Enhances Estrogen Receptor Function in vitro</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Target gene activation by nuclear hormone receptors, including estrogen receptors (ERs), is thought to be mediated by a variety of interacting cofactors. Here we identify a number of nuclear extract-derived proteins that interact with immobilized ER ligand binding domains in a 17β-estradiol-dependent manner. The most prominent of these are components of the thyroid hormone receptor-associated protein (TRAP)/Mediator coactivator complex, which interacts with ERα and ERβ in both unfractionated nuclear extracts and purified form. Studies with extracts from TRAP220-/-fibroblasts reveal that these interactions depend on TRAP220, a TRAP/Mediator subunit previously shown to interact with ER and other nuclear receptors in a ligand-dependent manner. The physiological relevance of the in vitro interaction is documented further by the isolation of an ERα-TRAP/Mediator complex from cultured cells expressing an epitope-tagged ERα. Finally, the complete TRAP/Mediator complex is shown to enhance ER function directly in a highly purified cell-free transcription system. These studies firmly establish a direct role for TRAP/Mediator, through TRAP220, in ER function.</description><subject>Animals</subject><subject>Antibodies</subject><subject>Biochemistry</subject><subject>Biological Sciences</subject><subject>Carrier Proteins - metabolism</subject><subject>Cell Extracts</subject><subject>Cell Line, Transformed</subject><subject>Cell lines</subject><subject>Cell Nucleus - metabolism</subject><subject>Drug interactions</subject><subject>Estradiol - pharmacology</subject><subject>Estrogen Receptor alpha</subject><subject>Estrogen Receptor beta</subject><subject>Estrogens</subject><subject>Genes</subject><subject>HeLa Cells</subject><subject>Hormones</subject><subject>Humans</subject><subject>Intracellular Fluid</subject><subject>Ligands</subject><subject>Mathematical functions</subject><subject>Mediator complex</subject><subject>Mediator Complex Subunit 1</subject><subject>Mice</subject><subject>Nuclear interactions</subject><subject>Nuclear receptors</subject><subject>Proteins</subject><subject>Receptors</subject><subject>Receptors, Estrogen - genetics</subject><subject>Receptors, Estrogen - metabolism</subject><subject>Receptors, Thyroid Hormone - metabolism</subject><subject>Recombinant Fusion Proteins - genetics</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Trans-Activators - metabolism</subject><subject>Transcription Factors</subject><subject>TRAP protein</subject><subject>TRAP220 gene</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFks9uEzEQxlcIREPhygkhiwO3Tcdee-09cKhCCpWKQCWcLdfrzTra2KntDfStgAfpM-GSKPw7cBrL8_tmxp6vKJ5imGLg1cnGqTglNeaYiaa5V0wwNLisaQP3iwkA4aWghB4Vj2JcAUDDBDwsjjAWNed1Mym-LnqDFpenH07emdaq5AOaeaWT3e7P681gvqBzl0zI1xG9tsHoNNygzzb1aB5T8Evj0KXRZpMVEd1-Q8q16PY7Sn3w47LPcdeCEEAfx6vR2fQTOZSau145beK_5dDZ6PIw3iHr0Nbm7OPiQaeGaJ7s43Hx6Wy-mL0tL96_OZ-dXpSa1jSVvG1r1XFQAlTDmSJKEw68MwKYaQ2wmileNbzqWsZYLRi0TBOMDcNUaEqr4-LVru5mvFqbVhuXghrkJti1CjfSKyv_zDjby6XfSkwIBZz1L_f64K9HE5Nc26jNMChn_BhlXlglaqD_BbEgnBJeZfDFX-DKj8HlT5AkN2wYxZCh6Q7SwccYTHeYGIO8c4y8c4w8OCYLnv_-zl_43iIZeLYDVjEv5JCvIFsJSPUD6e_J8Q</recordid><startdate>20020305</startdate><enddate>20020305</enddate><creator>Kang, Yun Kyoung</creator><creator>Guermah, Mohamed</creator><creator>Yuan, Chao-Xing</creator><creator>Roeder, Robert G.</creator><general>National Academy of Sciences</general><general>The National Academy of Sciences</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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20020305</creationdate><title>The TRAP/Mediator Coactivator Complex Interacts Directly with Estrogen Receptors α and β through the TRAP220 Subunit and Directly Enhances Estrogen Receptor Function in vitro</title><author>Kang, Yun Kyoung ; Guermah, Mohamed ; Yuan, Chao-Xing ; Roeder, Robert G.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c464t-7dd6af70a80a975a2ac2707fe805ede0565a73973fd5556850d5c211e5148c443</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Animals</topic><topic>Antibodies</topic><topic>Biochemistry</topic><topic>Biological Sciences</topic><topic>Carrier Proteins - metabolism</topic><topic>Cell Extracts</topic><topic>Cell Line, Transformed</topic><topic>Cell lines</topic><topic>Cell Nucleus - metabolism</topic><topic>Drug interactions</topic><topic>Estradiol - pharmacology</topic><topic>Estrogen Receptor alpha</topic><topic>Estrogen Receptor beta</topic><topic>Estrogens</topic><topic>Genes</topic><topic>HeLa Cells</topic><topic>Hormones</topic><topic>Humans</topic><topic>Intracellular Fluid</topic><topic>Ligands</topic><topic>Mathematical functions</topic><topic>Mediator complex</topic><topic>Mediator Complex Subunit 1</topic><topic>Mice</topic><topic>Nuclear interactions</topic><topic>Nuclear receptors</topic><topic>Proteins</topic><topic>Receptors</topic><topic>Receptors, Estrogen - genetics</topic><topic>Receptors, Estrogen - metabolism</topic><topic>Receptors, Thyroid Hormone - metabolism</topic><topic>Recombinant Fusion Proteins - genetics</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>Trans-Activators - metabolism</topic><topic>Transcription Factors</topic><topic>TRAP protein</topic><topic>TRAP220 gene</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kang, Yun Kyoung</creatorcontrib><creatorcontrib>Guermah, Mohamed</creatorcontrib><creatorcontrib>Yuan, Chao-Xing</creatorcontrib><creatorcontrib>Roeder, Robert G.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kang, Yun Kyoung</au><au>Guermah, Mohamed</au><au>Yuan, Chao-Xing</au><au>Roeder, Robert G.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The TRAP/Mediator Coactivator Complex Interacts Directly with Estrogen Receptors α and β through the TRAP220 Subunit and Directly Enhances Estrogen Receptor Function in vitro</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2002-03-05</date><risdate>2002</risdate><volume>99</volume><issue>5</issue><spage>2642</spage><epage>2647</epage><pages>2642-2647</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>Target gene activation by nuclear hormone receptors, including estrogen receptors (ERs), is thought to be mediated by a variety of interacting cofactors. Here we identify a number of nuclear extract-derived proteins that interact with immobilized ER ligand binding domains in a 17β-estradiol-dependent manner. The most prominent of these are components of the thyroid hormone receptor-associated protein (TRAP)/Mediator coactivator complex, which interacts with ERα and ERβ in both unfractionated nuclear extracts and purified form. Studies with extracts from TRAP220-/-fibroblasts reveal that these interactions depend on TRAP220, a TRAP/Mediator subunit previously shown to interact with ER and other nuclear receptors in a ligand-dependent manner. The physiological relevance of the in vitro interaction is documented further by the isolation of an ERα-TRAP/Mediator complex from cultured cells expressing an epitope-tagged ERα. Finally, the complete TRAP/Mediator complex is shown to enhance ER function directly in a highly purified cell-free transcription system. These studies firmly establish a direct role for TRAP/Mediator, through TRAP220, in ER function.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>11867769</pmid><doi>10.1073/pnas.261715899</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0027-8424 |
| ispartof | Proceedings of the National Academy of Sciences - PNAS, 2002-03, Vol.99 (5), p.2642-2647 |
| issn | 0027-8424 1091-6490 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_122401 |
| source | MEDLINE; Full-Text Journals in Chemistry (Open access); PubMed Central; Alma/SFX Local Collection; JSTOR |
| subjects | Animals Antibodies Biochemistry Biological Sciences Carrier Proteins - metabolism Cell Extracts Cell Line, Transformed Cell lines Cell Nucleus - metabolism Drug interactions Estradiol - pharmacology Estrogen Receptor alpha Estrogen Receptor beta Estrogens Genes HeLa Cells Hormones Humans Intracellular Fluid Ligands Mathematical functions Mediator complex Mediator Complex Subunit 1 Mice Nuclear interactions Nuclear receptors Proteins Receptors Receptors, Estrogen - genetics Receptors, Estrogen - metabolism Receptors, Thyroid Hormone - metabolism Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism Trans-Activators - metabolism Transcription Factors TRAP protein TRAP220 gene |
| title | The TRAP/Mediator Coactivator Complex Interacts Directly with Estrogen Receptors α and β through the TRAP220 Subunit and Directly Enhances Estrogen Receptor Function in vitro |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-07T19%3A09%3A41IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-jstor_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=The%20TRAP/Mediator%20Coactivator%20Complex%20Interacts%20Directly%20with%20Estrogen%20Receptors%20%CE%B1%20and%20%CE%B2%20through%20the%20TRAP220%20Subunit%20and%20Directly%20Enhances%20Estrogen%20Receptor%20Function%20in%20vitro&rft.jtitle=Proceedings%20of%20the%20National%20Academy%20of%20Sciences%20-%20PNAS&rft.au=Kang,%20Yun%20Kyoung&rft.date=2002-03-05&rft.volume=99&rft.issue=5&rft.spage=2642&rft.epage=2647&rft.pages=2642-2647&rft.issn=0027-8424&rft.eissn=1091-6490&rft_id=info:doi/10.1073/pnas.261715899&rft_dat=%3Cjstor_pubme%3E3058002%3C/jstor_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=201395410&rft_id=info:pmid/11867769&rft_jstor_id=3058002&rfr_iscdi=true |