DAF-16 Recruits the CREB-Binding Protein Coactivator Complex to the Insulin-Like Growth Factor Binding Protein 1 Promoter in HepG2 Cells
Insulin negatively regulates expression of the insulin-like growth factor binding protein 1 (IGFBP-1) gene by means of an insulin-responsive element (IRE) that also contributes to glucocorticoid stimulation of this gene. We find that the Caenorhabditis elegans protein DAF-16 binds the IGFBP-1· IRE w...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2000-09, Vol.97 (19), p.10412-10417 |
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| creator | Nasrin, Nargis Ogg, Scott Cahill, Catherine M. Biggs, William Nui, Simin Dore, Justin Calvo, Dominica Shi, Yang Ruvkun, Gary Alexander-Bridges, Maria C. |
| description | Insulin negatively regulates expression of the insulin-like growth factor binding protein 1 (IGFBP-1) gene by means of an insulin-responsive element (IRE) that also contributes to glucocorticoid stimulation of this gene. We find that the Caenorhabditis elegans protein DAF-16 binds the IGFBP-1· IRE with specificity similar to that of the forkhead (FKH) factor(s) that act both to enhance glucocorticoid responsiveness and to mediate the negative effect of insulin at this site. In HepG2 cells, DAF-16 and its mammalian homologs, FKHR, FKHRL1, and AFX, activate transcription through the IGFBP-1· IRE; this effect is inhibited by the viral oncoprotein E1A, but not by mutants of E1A that fail to interact with the coactivator p300/CREB-binding protein (CBP). We show that DAF-16 and FKHR can interact with both the KIX and E1A/SRC interaction domains of p300/CBP, as well as the steroid receptor coactivator (SRC). A C-terminal deletion mutant of DAF-16 that is nonfunctional in C. elegans fails to bind the KIX domain of CBP, fails to activate transcription through the IGFBP-1· IRE, and inhibits activation of the IGFBP-1 promoter by glucocorticoids. Thus, the interaction of DAF-16 homologs with the KIX domain of CBP is essential to basal and glucocorticoid-stimulated transactivation. Although AFX interacts with the KIX domain of CBP, it does not interact with SRC and does not respond to glucocorticoids or insulin. Thus, we conclude that DAF-16 and FKHR act as accessory factors to the glucocorticoid response, by recruiting the p300/CBP/SRC coactivator complex to an FKH factor site in the IGFBP-1 promoter, which allows the cell to integrate the effects of glucocorticoids and insulin on genes that carry this site. |
| doi_str_mv | 10.1073/pnas.190326997 |
| format | Article |
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We find that the Caenorhabditis elegans protein DAF-16 binds the IGFBP-1· IRE with specificity similar to that of the forkhead (FKH) factor(s) that act both to enhance glucocorticoid responsiveness and to mediate the negative effect of insulin at this site. In HepG2 cells, DAF-16 and its mammalian homologs, FKHR, FKHRL1, and AFX, activate transcription through the IGFBP-1· IRE; this effect is inhibited by the viral oncoprotein E1A, but not by mutants of E1A that fail to interact with the coactivator p300/CREB-binding protein (CBP). We show that DAF-16 and FKHR can interact with both the KIX and E1A/SRC interaction domains of p300/CBP, as well as the steroid receptor coactivator (SRC). A C-terminal deletion mutant of DAF-16 that is nonfunctional in C. elegans fails to bind the KIX domain of CBP, fails to activate transcription through the IGFBP-1· IRE, and inhibits activation of the IGFBP-1 promoter by glucocorticoids. Thus, the interaction of DAF-16 homologs with the KIX domain of CBP is essential to basal and glucocorticoid-stimulated transactivation. Although AFX interacts with the KIX domain of CBP, it does not interact with SRC and does not respond to glucocorticoids or insulin. Thus, we conclude that DAF-16 and FKHR act as accessory factors to the glucocorticoid response, by recruiting the p300/CBP/SRC coactivator complex to an FKH factor site in the IGFBP-1 promoter, which allows the cell to integrate the effects of glucocorticoids and insulin on genes that carry this site.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.190326997</identifier><identifier>PMID: 10973497</identifier><language>eng</language><publisher>United States: National Academy of Sciences of the United States of America</publisher><subject>Adenovirus E1A Proteins - metabolism ; AFX protein ; Amino acids ; Base Sequence ; Biological Sciences ; Caenorhabditis elegans ; Caenorhabditis elegans Proteins ; Cellular biology ; Chemical bonds ; CREB-Binding Protein ; DAF-16 protein ; DNA Primers ; E1A protein ; FKHR protein ; FKHRL1 protein ; forkhead protein ; Forkhead Transcription Factors ; Gene expression ; Gene Expression Regulation - drug effects ; Genes ; Genetic vectors ; Glucocorticoids ; Glucocorticoids - pharmacology ; HEK293 cells ; Hep G2 cells ; Humans ; Insulin ; Insulin - pharmacology ; insulin-like growth factor binding protein 1 ; Insulin-Like Growth Factor Binding Protein 1 - genetics ; Nuclear Proteins - metabolism ; p300 protein ; Promoter Regions, Genetic ; Protein Binding ; Proteins ; steroid receptor coactivator ; Trans-Activators - metabolism ; Transcription Factors - metabolism ; Transcription, Genetic - drug effects ; Tumor Cells, Cultured ; Yeasts</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2000-09, Vol.97 (19), p.10412-10417</ispartof><rights>Copyright 1993-2000 National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences Sep 12, 2000</rights><rights>Copyright © 2000, The National Academy of Sciences 2000</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c587t-f47f697881ef8b11ac8005ba0882ae845a3c0e01395d8854d78296d9b60170de3</citedby><cites>FETCH-LOGICAL-c587t-f47f697881ef8b11ac8005ba0882ae845a3c0e01395d8854d78296d9b60170de3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/97/19.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/123575$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/123575$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,724,777,781,800,882,27905,27906,53772,53774,57998,58231</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10973497$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Nasrin, Nargis</creatorcontrib><creatorcontrib>Ogg, Scott</creatorcontrib><creatorcontrib>Cahill, Catherine M.</creatorcontrib><creatorcontrib>Biggs, William</creatorcontrib><creatorcontrib>Nui, Simin</creatorcontrib><creatorcontrib>Dore, Justin</creatorcontrib><creatorcontrib>Calvo, Dominica</creatorcontrib><creatorcontrib>Shi, Yang</creatorcontrib><creatorcontrib>Ruvkun, Gary</creatorcontrib><creatorcontrib>Alexander-Bridges, Maria C.</creatorcontrib><title>DAF-16 Recruits the CREB-Binding Protein Coactivator Complex to the Insulin-Like Growth Factor Binding Protein 1 Promoter in HepG2 Cells</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Insulin negatively regulates expression of the insulin-like growth factor binding protein 1 (IGFBP-1) gene by means of an insulin-responsive element (IRE) that also contributes to glucocorticoid stimulation of this gene. We find that the Caenorhabditis elegans protein DAF-16 binds the IGFBP-1· IRE with specificity similar to that of the forkhead (FKH) factor(s) that act both to enhance glucocorticoid responsiveness and to mediate the negative effect of insulin at this site. In HepG2 cells, DAF-16 and its mammalian homologs, FKHR, FKHRL1, and AFX, activate transcription through the IGFBP-1· IRE; this effect is inhibited by the viral oncoprotein E1A, but not by mutants of E1A that fail to interact with the coactivator p300/CREB-binding protein (CBP). We show that DAF-16 and FKHR can interact with both the KIX and E1A/SRC interaction domains of p300/CBP, as well as the steroid receptor coactivator (SRC). A C-terminal deletion mutant of DAF-16 that is nonfunctional in C. elegans fails to bind the KIX domain of CBP, fails to activate transcription through the IGFBP-1· IRE, and inhibits activation of the IGFBP-1 promoter by glucocorticoids. Thus, the interaction of DAF-16 homologs with the KIX domain of CBP is essential to basal and glucocorticoid-stimulated transactivation. Although AFX interacts with the KIX domain of CBP, it does not interact with SRC and does not respond to glucocorticoids or insulin. Thus, we conclude that DAF-16 and FKHR act as accessory factors to the glucocorticoid response, by recruiting the p300/CBP/SRC coactivator complex to an FKH factor site in the IGFBP-1 promoter, which allows the cell to integrate the effects of glucocorticoids and insulin on genes that carry this site.</description><subject>Adenovirus E1A Proteins - metabolism</subject><subject>AFX protein</subject><subject>Amino acids</subject><subject>Base Sequence</subject><subject>Biological Sciences</subject><subject>Caenorhabditis elegans</subject><subject>Caenorhabditis elegans Proteins</subject><subject>Cellular biology</subject><subject>Chemical bonds</subject><subject>CREB-Binding Protein</subject><subject>DAF-16 protein</subject><subject>DNA Primers</subject><subject>E1A protein</subject><subject>FKHR protein</subject><subject>FKHRL1 protein</subject><subject>forkhead protein</subject><subject>Forkhead Transcription Factors</subject><subject>Gene expression</subject><subject>Gene Expression Regulation - drug effects</subject><subject>Genes</subject><subject>Genetic vectors</subject><subject>Glucocorticoids</subject><subject>Glucocorticoids - pharmacology</subject><subject>HEK293 cells</subject><subject>Hep G2 cells</subject><subject>Humans</subject><subject>Insulin</subject><subject>Insulin - pharmacology</subject><subject>insulin-like growth factor binding protein 1</subject><subject>Insulin-Like Growth Factor Binding Protein 1 - genetics</subject><subject>Nuclear Proteins - metabolism</subject><subject>p300 protein</subject><subject>Promoter Regions, Genetic</subject><subject>Protein Binding</subject><subject>Proteins</subject><subject>steroid receptor coactivator</subject><subject>Trans-Activators - metabolism</subject><subject>Transcription Factors - metabolism</subject><subject>Transcription, Genetic - drug effects</subject><subject>Tumor Cells, Cultured</subject><subject>Yeasts</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0kFv0zAUAOAIgVgZXLkggcUBcUl5dpzYlrhsYe0mVQJNcLbcxFldUjuznbH9g_1sXFrG2AFOfpa_95wXvyx7iWGKgRUfBqvCFAsoSCUEe5RNMAicV1TA42wCQFjOKaEH2bMQ1gAgSg5Ps4OEWEEFm2S3n45mOa7QuW78aGJAcaVRfX5ynB8b2xp7gb54F7WxqHaqieZKRedTvBl6fY2i--XPbBh7Y_OF-a7R3LsfcYVmSSf5sAreRpsUe5R2p3qYE1Trvg_Psyed6oN-sV8Ps2-zk6_1ab74PD-rjxZ5U3IW846yrhKMc6w7vsRYNRygXCrgnCjNaamKBjTgQpQt5yVtGSeiasWyAsyg1cVh9nFXdxiXG9022kavejl4s1H-Rjpl5N8n1qzkhbuShEHBU_q7fbp3l6MOUW5MaFIDymo3BskIKTmn4r8Qs6ogADTBtw_g2o3epn8gSeqj4hiThKY71HgXgtfd3QdjkNtBkNtBkHeDkBJe32_zHt-9fALv92Cb-PtYsFQjIYqJ7Ma-j_o6Jvrm3zSJVzuxDunR_1xGipKVxU8t589m</recordid><startdate>20000912</startdate><enddate>20000912</enddate><creator>Nasrin, Nargis</creator><creator>Ogg, Scott</creator><creator>Cahill, Catherine M.</creator><creator>Biggs, William</creator><creator>Nui, Simin</creator><creator>Dore, Justin</creator><creator>Calvo, Dominica</creator><creator>Shi, Yang</creator><creator>Ruvkun, Gary</creator><creator>Alexander-Bridges, Maria C.</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</general><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>20000912</creationdate><title>DAF-16 Recruits the CREB-Binding Protein Coactivator Complex to the Insulin-Like Growth Factor Binding Protein 1 Promoter in HepG2 Cells</title><author>Nasrin, Nargis ; 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We find that the Caenorhabditis elegans protein DAF-16 binds the IGFBP-1· IRE with specificity similar to that of the forkhead (FKH) factor(s) that act both to enhance glucocorticoid responsiveness and to mediate the negative effect of insulin at this site. In HepG2 cells, DAF-16 and its mammalian homologs, FKHR, FKHRL1, and AFX, activate transcription through the IGFBP-1· IRE; this effect is inhibited by the viral oncoprotein E1A, but not by mutants of E1A that fail to interact with the coactivator p300/CREB-binding protein (CBP). We show that DAF-16 and FKHR can interact with both the KIX and E1A/SRC interaction domains of p300/CBP, as well as the steroid receptor coactivator (SRC). A C-terminal deletion mutant of DAF-16 that is nonfunctional in C. elegans fails to bind the KIX domain of CBP, fails to activate transcription through the IGFBP-1· IRE, and inhibits activation of the IGFBP-1 promoter by glucocorticoids. Thus, the interaction of DAF-16 homologs with the KIX domain of CBP is essential to basal and glucocorticoid-stimulated transactivation. Although AFX interacts with the KIX domain of CBP, it does not interact with SRC and does not respond to glucocorticoids or insulin. Thus, we conclude that DAF-16 and FKHR act as accessory factors to the glucocorticoid response, by recruiting the p300/CBP/SRC coactivator complex to an FKH factor site in the IGFBP-1 promoter, which allows the cell to integrate the effects of glucocorticoids and insulin on genes that carry this site.</abstract><cop>United States</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>10973497</pmid><doi>10.1073/pnas.190326997</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Proceedings of the National Academy of Sciences - PNAS, 2000-09, Vol.97 (19), p.10412-10417 |
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| subjects | Adenovirus E1A Proteins - metabolism AFX protein Amino acids Base Sequence Biological Sciences Caenorhabditis elegans Caenorhabditis elegans Proteins Cellular biology Chemical bonds CREB-Binding Protein DAF-16 protein DNA Primers E1A protein FKHR protein FKHRL1 protein forkhead protein Forkhead Transcription Factors Gene expression Gene Expression Regulation - drug effects Genes Genetic vectors Glucocorticoids Glucocorticoids - pharmacology HEK293 cells Hep G2 cells Humans Insulin Insulin - pharmacology insulin-like growth factor binding protein 1 Insulin-Like Growth Factor Binding Protein 1 - genetics Nuclear Proteins - metabolism p300 protein Promoter Regions, Genetic Protein Binding Proteins steroid receptor coactivator Trans-Activators - metabolism Transcription Factors - metabolism Transcription, Genetic - drug effects Tumor Cells, Cultured Yeasts |
| title | DAF-16 Recruits the CREB-Binding Protein Coactivator Complex to the Insulin-Like Growth Factor Binding Protein 1 Promoter in HepG2 Cells |
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