Suppression of FOXO1 activity by FHL2 through SIRT1-mediated deacetylation
Forkhead box class O (FOXO) proteins are transcription factors that function downstream of the PTEN tumor suppressor and directly control the expression of genes involved in apoptosis, cell cycle progression, and stress responses. In the present study, we show that FOXO1 interacts with four and a ha...
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| Veröffentlicht in: | The EMBO journal 2005-03, Vol.24 (5), p.1021-1032 |
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| creator | Yang, Yonghua Hou, Huayan Haller, Edward M Nicosia, Santo V Bai, Wenlong |
| description | Forkhead box class O (FOXO) proteins are transcription factors that function downstream of the PTEN tumor suppressor and directly control the expression of genes involved in apoptosis, cell cycle progression, and stress responses. In the present study, we show that FOXO1 interacts with four and a half LIM 2 (FHL2) in prostate cancer cells. This interaction occurred in the nucleus and was enhanced by lysophosphatic acid. FHL2 decreased the transcriptional activity of FOXO1 and the expression of known FOXO target genes and inhibited FOXO1‐induced apoptosis. Interestingly, SIRT1, a mammalian homolog of yeast Sir2, bound to and deacetylated FOXO1 and inhibited its transcriptional activity. FHL2 enhanced the interaction of FOXO1 and SIRT1 and the deacetylation of FOXO1 by Sirtuin‐1 (SIRT1). Overall, our data show that FHL2 inhibits FOXO1 activity in prostate cancer cells by promoting the deacetylation of FOXO1 by SIRT1. |
| doi_str_mv | 10.1038/sj.emboj.7600570 |
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In the present study, we show that FOXO1 interacts with four and a half LIM 2 (FHL2) in prostate cancer cells. This interaction occurred in the nucleus and was enhanced by lysophosphatic acid. FHL2 decreased the transcriptional activity of FOXO1 and the expression of known FOXO target genes and inhibited FOXO1‐induced apoptosis. Interestingly, SIRT1, a mammalian homolog of yeast Sir2, bound to and deacetylated FOXO1 and inhibited its transcriptional activity. FHL2 enhanced the interaction of FOXO1 and SIRT1 and the deacetylation of FOXO1 by Sirtuin‐1 (SIRT1). Overall, our data show that FHL2 inhibits FOXO1 activity in prostate cancer cells by promoting the deacetylation of FOXO1 by SIRT1.</description><identifier>ISSN: 0261-4189</identifier><identifier>EISSN: 1460-2075</identifier><identifier>DOI: 10.1038/sj.emboj.7600570</identifier><identifier>PMID: 15692560</identifier><identifier>CODEN: EMJODG</identifier><language>eng</language><publisher>Chichester, UK: John Wiley & Sons, Ltd</publisher><subject>Acetylation ; Apoptosis ; Base Sequence ; Cell Line, Tumor ; Cell Nucleus - drug effects ; Cell Nucleus - metabolism ; DNA, Neoplasm - genetics ; DNA, Neoplasm - metabolism ; DNA-Binding Proteins - antagonists & inhibitors ; DNA-Binding Proteins - genetics ; DNA-Binding Proteins - metabolism ; EMBO09 ; EMBO24 ; FKHR ; forkhead ; Forkhead Box Protein O1 ; Forkhead Transcription Factors ; Histone Deacetylases - metabolism ; Homeodomain Proteins - metabolism ; Humans ; LIM-Homeodomain Proteins ; Lysophospholipids - pharmacology ; Male ; Mammals ; Models, Biological ; Muscle Proteins - metabolism ; Prostate cancer ; Prostatic Neoplasms - genetics ; Prostatic Neoplasms - metabolism ; Prostatic Neoplasms - pathology ; SIR2 ; Sirtuin 1 ; Sirtuins - metabolism ; Transcription Factors - antagonists & inhibitors ; Transcription Factors - genetics ; Transcription Factors - metabolism ; Transcription, Genetic ; Two-Hybrid System Techniques ; Yeasts</subject><ispartof>The EMBO journal, 2005-03, Vol.24 (5), p.1021-1032</ispartof><rights>European Molecular Biology Organization 2005</rights><rights>Copyright © 2005 European Molecular Biology Organization</rights><rights>Copyright Nature Publishing Group Mar 9, 2005</rights><rights>Copyright © 2005, European Molecular Biology Organization 2005</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c6470-e1232033781f10aa2e8fc27d28d603f9343e00ad0ed36364338d8b259a500c1a3</citedby><cites>FETCH-LOGICAL-c6470-e1232033781f10aa2e8fc27d28d603f9343e00ad0ed36364338d8b259a500c1a3</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/PMC554122/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC554122/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,1411,1427,27903,27904,41099,42168,45553,45554,46388,46812,51555,53770,53772</link.rule.ids><linktorsrc>$$Uhttps://doi.org/10.1038/sj.emboj.7600570$$EView_record_in_Springer_Nature$$FView_record_in_$$GSpringer_Nature</linktorsrc><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15692560$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yang, Yonghua</creatorcontrib><creatorcontrib>Hou, Huayan</creatorcontrib><creatorcontrib>Haller, Edward M</creatorcontrib><creatorcontrib>Nicosia, Santo V</creatorcontrib><creatorcontrib>Bai, Wenlong</creatorcontrib><title>Suppression of FOXO1 activity by FHL2 through SIRT1-mediated deacetylation</title><title>The EMBO journal</title><addtitle>EMBO J</addtitle><addtitle>EMBO J</addtitle><description>Forkhead box class O (FOXO) proteins are transcription factors that function downstream of the PTEN tumor suppressor and directly control the expression of genes involved in apoptosis, cell cycle progression, and stress responses. In the present study, we show that FOXO1 interacts with four and a half LIM 2 (FHL2) in prostate cancer cells. This interaction occurred in the nucleus and was enhanced by lysophosphatic acid. FHL2 decreased the transcriptional activity of FOXO1 and the expression of known FOXO target genes and inhibited FOXO1‐induced apoptosis. Interestingly, SIRT1, a mammalian homolog of yeast Sir2, bound to and deacetylated FOXO1 and inhibited its transcriptional activity. FHL2 enhanced the interaction of FOXO1 and SIRT1 and the deacetylation of FOXO1 by Sirtuin‐1 (SIRT1). Overall, our data show that FHL2 inhibits FOXO1 activity in prostate cancer cells by promoting the deacetylation of FOXO1 by SIRT1.</description><subject>Acetylation</subject><subject>Apoptosis</subject><subject>Base Sequence</subject><subject>Cell Line, Tumor</subject><subject>Cell Nucleus - drug effects</subject><subject>Cell Nucleus - metabolism</subject><subject>DNA, Neoplasm - genetics</subject><subject>DNA, Neoplasm - metabolism</subject><subject>DNA-Binding Proteins - antagonists & inhibitors</subject><subject>DNA-Binding Proteins - genetics</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>EMBO09</subject><subject>EMBO24</subject><subject>FKHR</subject><subject>forkhead</subject><subject>Forkhead Box Protein O1</subject><subject>Forkhead Transcription Factors</subject><subject>Histone Deacetylases - metabolism</subject><subject>Homeodomain Proteins - metabolism</subject><subject>Humans</subject><subject>LIM-Homeodomain Proteins</subject><subject>Lysophospholipids - pharmacology</subject><subject>Male</subject><subject>Mammals</subject><subject>Models, Biological</subject><subject>Muscle Proteins - metabolism</subject><subject>Prostate cancer</subject><subject>Prostatic Neoplasms - genetics</subject><subject>Prostatic Neoplasms - metabolism</subject><subject>Prostatic Neoplasms - pathology</subject><subject>SIR2</subject><subject>Sirtuin 1</subject><subject>Sirtuins - metabolism</subject><subject>Transcription Factors - antagonists & inhibitors</subject><subject>Transcription Factors - genetics</subject><subject>Transcription Factors - metabolism</subject><subject>Transcription, Genetic</subject><subject>Two-Hybrid System Techniques</subject><subject>Yeasts</subject><issn>0261-4189</issn><issn>1460-2075</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqFkc1v0zAYhy0EYmVw54QiDtxSXtvxRw4cYFq7TWUFNj5ulps4rUMaFzsZ5L_HI9U2kNBOPvh5fn79_hB6jmGKgcrXoZ6a7crVU8EBmIAHaIIzDikBwR6iCRCO0wzL_AA9CaGGyEiBH6MDzHhOGIcJOrvodztvQrCuTVyVzJbfljjRRWevbDckqyGZnSxI0m2869eb5OL00yVOt6a0ujNlUhpdmG5odBf1p-hRpZtgnu3PQ_R5dnx5dJIulvPTo7eLtOCZgNRgQglQKiSuMGhNjKwKIkoiSw60ymlGDYAuwZSUU55RKku5IizXDKDAmh6iN2Purl_FSQrTdl43auftVvtBOW3V3zet3ai1u1KMZZiQ6L_a-9796E3o1NaGwjSNbo3rg-IiyznJ7gexYFRiKSL48h-wdr1v4xIUzhnhhIvrNBihwrsQvKluJsagrttUoVZ_2lT7NqPy4u5Pb4V9fRHIR-Cnbcxwb6A6fv_u7DYcj26IWrs2_s7Q_x8oHR0bOvPr5j3tv8etUcHU1_O5mkdVfDj_oj7S3wcVzI0</recordid><startdate>20050309</startdate><enddate>20050309</enddate><creator>Yang, Yonghua</creator><creator>Hou, Huayan</creator><creator>Haller, Edward M</creator><creator>Nicosia, Santo V</creator><creator>Bai, Wenlong</creator><general>John Wiley & Sons, Ltd</general><general>Nature Publishing Group UK</general><general>Blackwell Publishing Ltd</general><scope>BSCLL</scope><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>7QP</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PCBAR</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20050309</creationdate><title>Suppression of FOXO1 activity by FHL2 through SIRT1-mediated deacetylation</title><author>Yang, Yonghua ; Hou, Huayan ; Haller, Edward M ; Nicosia, Santo V ; Bai, Wenlong</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c6470-e1232033781f10aa2e8fc27d28d603f9343e00ad0ed36364338d8b259a500c1a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Acetylation</topic><topic>Apoptosis</topic><topic>Base Sequence</topic><topic>Cell Line, Tumor</topic><topic>Cell Nucleus - 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The EMBO journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext_linktorsrc</fulltext></delivery><addata><au>Yang, Yonghua</au><au>Hou, Huayan</au><au>Haller, Edward M</au><au>Nicosia, Santo V</au><au>Bai, Wenlong</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Suppression of FOXO1 activity by FHL2 through SIRT1-mediated deacetylation</atitle><jtitle>The EMBO journal</jtitle><stitle>EMBO J</stitle><addtitle>EMBO J</addtitle><date>2005-03-09</date><risdate>2005</risdate><volume>24</volume><issue>5</issue><spage>1021</spage><epage>1032</epage><pages>1021-1032</pages><issn>0261-4189</issn><eissn>1460-2075</eissn><coden>EMJODG</coden><abstract>Forkhead box class O (FOXO) proteins are transcription factors that function downstream of the PTEN tumor suppressor and directly control the expression of genes involved in apoptosis, cell cycle progression, and stress responses. In the present study, we show that FOXO1 interacts with four and a half LIM 2 (FHL2) in prostate cancer cells. This interaction occurred in the nucleus and was enhanced by lysophosphatic acid. FHL2 decreased the transcriptional activity of FOXO1 and the expression of known FOXO target genes and inhibited FOXO1‐induced apoptosis. Interestingly, SIRT1, a mammalian homolog of yeast Sir2, bound to and deacetylated FOXO1 and inhibited its transcriptional activity. FHL2 enhanced the interaction of FOXO1 and SIRT1 and the deacetylation of FOXO1 by Sirtuin‐1 (SIRT1). Overall, our data show that FHL2 inhibits FOXO1 activity in prostate cancer cells by promoting the deacetylation of FOXO1 by SIRT1.</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><pmid>15692560</pmid><doi>10.1038/sj.emboj.7600570</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Acetylation Apoptosis Base Sequence Cell Line, Tumor Cell Nucleus - drug effects Cell Nucleus - metabolism DNA, Neoplasm - genetics DNA, Neoplasm - metabolism DNA-Binding Proteins - antagonists & inhibitors DNA-Binding Proteins - genetics DNA-Binding Proteins - metabolism EMBO09 EMBO24 FKHR forkhead Forkhead Box Protein O1 Forkhead Transcription Factors Histone Deacetylases - metabolism Homeodomain Proteins - metabolism Humans LIM-Homeodomain Proteins Lysophospholipids - pharmacology Male Mammals Models, Biological Muscle Proteins - metabolism Prostate cancer Prostatic Neoplasms - genetics Prostatic Neoplasms - metabolism Prostatic Neoplasms - pathology SIR2 Sirtuin 1 Sirtuins - metabolism Transcription Factors - antagonists & inhibitors Transcription Factors - genetics Transcription Factors - metabolism Transcription, Genetic Two-Hybrid System Techniques Yeasts |
| title | Suppression of FOXO1 activity by FHL2 through SIRT1-mediated deacetylation |
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