SUG-1 Plays Proteolytic and Non-proteolytic Roles in the Control of Retinoic Acid Target Genes via Its Interaction with SRC-3
Nuclear retinoic acid receptor α (RARα) activates gene expression through dynamic interactions with coregulatory protein complexes, the assembly of which is directed by the ligand and the AF-2 domain of RARα. Then RARα and its coactivator SRC-3 are degraded by the proteasome. Recently it has emerged...
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| Veröffentlicht in: | The Journal of biological chemistry 2009-03, Vol.284 (12), p.8127-8135 |
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| creator | Ferry, Christine Gianni, Maurizio Lalevée, Sébastien Bruck, Nathalie Plassat, Jean-Luc Raska, Ivan Garattini, Enrico Rochette-Egly, Cécile |
| description | Nuclear retinoic acid receptor α (RARα) activates gene expression through dynamic interactions with coregulatory protein complexes, the assembly of which is directed by the ligand and the AF-2 domain of RARα. Then RARα and its coactivator SRC-3 are degraded by the proteasome. Recently it has emerged that the proteasome also plays a key role in RARα-mediated transcription. Here we show that SUG-1, one of the six ATPases of the 19 S regulatory complex of the 26 S proteasome, interacts with SRC-3, is recruited at the promoters of retinoic acid (RA) target genes, and thereby participates to their transcription. In addition, SUG-1 also mediates the proteasomal degradation of SRC-3. However, when present in excess amounts, SUG-1 blocks the activation of RARα target genes and the degradation of RARα that occurs in response to RA, via its ability to interfere with the recruitment of SRC-3 and other coregulators at the AF-2 domain of RARα. We propose a model in which the ratio between SUG-1 and SRC-3 is crucial for the control of RARα functioning. This study provides new insights into how SUG-1 has a unique role in linking the transcription and degradation processes via its ability to interact with SRC-3. |
| doi_str_mv | 10.1074/jbc.M808815200 |
| format | Article |
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Then RARα and its coactivator SRC-3 are degraded by the proteasome. Recently it has emerged that the proteasome also plays a key role in RARα-mediated transcription. Here we show that SUG-1, one of the six ATPases of the 19 S regulatory complex of the 26 S proteasome, interacts with SRC-3, is recruited at the promoters of retinoic acid (RA) target genes, and thereby participates to their transcription. In addition, SUG-1 also mediates the proteasomal degradation of SRC-3. However, when present in excess amounts, SUG-1 blocks the activation of RARα target genes and the degradation of RARα that occurs in response to RA, via its ability to interfere with the recruitment of SRC-3 and other coregulators at the AF-2 domain of RARα. We propose a model in which the ratio between SUG-1 and SRC-3 is crucial for the control of RARα functioning. This study provides new insights into how SUG-1 has a unique role in linking the transcription and degradation processes via its ability to interact with SRC-3.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M808815200</identifier><identifier>PMID: 19144644</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Adaptor Proteins, Signal Transducing - genetics ; Adaptor Proteins, Signal Transducing - metabolism ; Animals ; ATPases Associated with Diverse Cellular Activities ; Chlorocebus aethiops ; COS Cells ; Gene Expression Regulation - drug effects ; Gene Expression Regulation - physiology ; HeLa Cells ; Histone Acetyltransferases - genetics ; Histone Acetyltransferases - metabolism ; Humans ; LIM Domain Proteins ; Models, Biological ; Nuclear Receptor Coactivator 3 ; Proteasome Endopeptidase Complex - metabolism ; Protein Structure, Tertiary - physiology ; Protein Synthesis, Post-Translational Modification, and Degradation ; Receptors, Retinoic Acid - genetics ; Receptors, Retinoic Acid - metabolism ; Retinoic Acid Receptor alpha ; Trans-Activators - genetics ; Trans-Activators - metabolism ; Transcription Factors - genetics ; Transcription Factors - metabolism ; Transcription, Genetic - drug effects ; Transcription, Genetic - physiology ; Tretinoin - pharmacology</subject><ispartof>The Journal of biological chemistry, 2009-03, Vol.284 (12), p.8127-8135</ispartof><rights>2009 © 2009 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><rights>Copyright © 2009, The American Society for Biochemistry and Molecular Biology, Inc.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c557t-29da51fbe1ee772d62cb602292902ee97b5550f8d6c847a9f202f8d543fda8813</citedby><cites>FETCH-LOGICAL-c557t-29da51fbe1ee772d62cb602292902ee97b5550f8d6c847a9f202f8d543fda8813</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/PMC2658106/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2658106/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27903,27904,53769,53771</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19144644$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://inserm.hal.science/inserm-00383334$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Ferry, Christine</creatorcontrib><creatorcontrib>Gianni, Maurizio</creatorcontrib><creatorcontrib>Lalevée, Sébastien</creatorcontrib><creatorcontrib>Bruck, Nathalie</creatorcontrib><creatorcontrib>Plassat, Jean-Luc</creatorcontrib><creatorcontrib>Raska, Ivan</creatorcontrib><creatorcontrib>Garattini, Enrico</creatorcontrib><creatorcontrib>Rochette-Egly, Cécile</creatorcontrib><title>SUG-1 Plays Proteolytic and Non-proteolytic Roles in the Control of Retinoic Acid Target Genes via Its Interaction with SRC-3</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Nuclear retinoic acid receptor α (RARα) activates gene expression through dynamic interactions with coregulatory protein complexes, the assembly of which is directed by the ligand and the AF-2 domain of RARα. 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Gianni, Maurizio ; Lalevée, Sébastien ; Bruck, Nathalie ; Plassat, Jean-Luc ; Raska, Ivan ; Garattini, Enrico ; Rochette-Egly, Cécile</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c557t-29da51fbe1ee772d62cb602292902ee97b5550f8d6c847a9f202f8d543fda8813</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Adaptor Proteins, Signal Transducing - genetics</topic><topic>Adaptor Proteins, Signal Transducing - metabolism</topic><topic>Animals</topic><topic>ATPases Associated with Diverse Cellular Activities</topic><topic>Chlorocebus aethiops</topic><topic>COS Cells</topic><topic>Gene Expression Regulation - drug effects</topic><topic>Gene Expression Regulation - physiology</topic><topic>HeLa Cells</topic><topic>Histone Acetyltransferases - genetics</topic><topic>Histone Acetyltransferases - metabolism</topic><topic>Humans</topic><topic>LIM Domain Proteins</topic><topic>Models, Biological</topic><topic>Nuclear Receptor Coactivator 3</topic><topic>Proteasome Endopeptidase Complex - metabolism</topic><topic>Protein Structure, Tertiary - physiology</topic><topic>Protein Synthesis, Post-Translational Modification, and Degradation</topic><topic>Receptors, Retinoic Acid - genetics</topic><topic>Receptors, Retinoic Acid - metabolism</topic><topic>Retinoic Acid Receptor alpha</topic><topic>Trans-Activators - genetics</topic><topic>Trans-Activators - metabolism</topic><topic>Transcription Factors - genetics</topic><topic>Transcription Factors - metabolism</topic><topic>Transcription, Genetic - drug effects</topic><topic>Transcription, Genetic - physiology</topic><topic>Tretinoin - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ferry, Christine</creatorcontrib><creatorcontrib>Gianni, Maurizio</creatorcontrib><creatorcontrib>Lalevée, Sébastien</creatorcontrib><creatorcontrib>Bruck, Nathalie</creatorcontrib><creatorcontrib>Plassat, Jean-Luc</creatorcontrib><creatorcontrib>Raska, Ivan</creatorcontrib><creatorcontrib>Garattini, Enrico</creatorcontrib><creatorcontrib>Rochette-Egly, Cécile</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>Hyper Article en Ligne (HAL)</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ferry, Christine</au><au>Gianni, Maurizio</au><au>Lalevée, Sébastien</au><au>Bruck, Nathalie</au><au>Plassat, Jean-Luc</au><au>Raska, Ivan</au><au>Garattini, Enrico</au><au>Rochette-Egly, Cécile</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>SUG-1 Plays Proteolytic and Non-proteolytic Roles in the Control of Retinoic Acid Target Genes via Its Interaction with SRC-3</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2009-03-20</date><risdate>2009</risdate><volume>284</volume><issue>12</issue><spage>8127</spage><epage>8135</epage><pages>8127-8135</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Nuclear retinoic acid receptor α (RARα) activates gene expression through dynamic interactions with coregulatory protein complexes, the assembly of which is directed by the ligand and the AF-2 domain of RARα. Then RARα and its coactivator SRC-3 are degraded by the proteasome. Recently it has emerged that the proteasome also plays a key role in RARα-mediated transcription. Here we show that SUG-1, one of the six ATPases of the 19 S regulatory complex of the 26 S proteasome, interacts with SRC-3, is recruited at the promoters of retinoic acid (RA) target genes, and thereby participates to their transcription. In addition, SUG-1 also mediates the proteasomal degradation of SRC-3. However, when present in excess amounts, SUG-1 blocks the activation of RARα target genes and the degradation of RARα that occurs in response to RA, via its ability to interfere with the recruitment of SRC-3 and other coregulators at the AF-2 domain of RARα. We propose a model in which the ratio between SUG-1 and SRC-3 is crucial for the control of RARα functioning. This study provides new insights into how SUG-1 has a unique role in linking the transcription and degradation processes via its ability to interact with SRC-3.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>19144644</pmid><doi>10.1074/jbc.M808815200</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Adaptor Proteins, Signal Transducing - genetics Adaptor Proteins, Signal Transducing - metabolism Animals ATPases Associated with Diverse Cellular Activities Chlorocebus aethiops COS Cells Gene Expression Regulation - drug effects Gene Expression Regulation - physiology HeLa Cells Histone Acetyltransferases - genetics Histone Acetyltransferases - metabolism Humans LIM Domain Proteins Models, Biological Nuclear Receptor Coactivator 3 Proteasome Endopeptidase Complex - metabolism Protein Structure, Tertiary - physiology Protein Synthesis, Post-Translational Modification, and Degradation Receptors, Retinoic Acid - genetics Receptors, Retinoic Acid - metabolism Retinoic Acid Receptor alpha Trans-Activators - genetics Trans-Activators - metabolism Transcription Factors - genetics Transcription Factors - metabolism Transcription, Genetic - drug effects Transcription, Genetic - physiology Tretinoin - pharmacology |
| title | SUG-1 Plays Proteolytic and Non-proteolytic Roles in the Control of Retinoic Acid Target Genes via Its Interaction with SRC-3 |
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