Regulation of E2F1 Function by the Nuclear Corepressor KAP1
KAP1 is a nuclear corepressor with conserved domains for RING finger, B boxes, leucine zipper α helical coiled-coil region, plant homeo domain finger, and bromo domain. The plant homeo domain finger and bromo domain of KAP1 cooperatively function as a transcription repression domain by recruiting th...
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| Veröffentlicht in: | The Journal of biological chemistry 2007-10, Vol.282 (41), p.29902-29909 |
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| container_issue | 41 |
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| container_title | The Journal of biological chemistry |
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| creator | Wang, Chuangui Rauscher, Frank J. Cress, W. Douglas Chen, Jiandong |
| description | KAP1 is a nuclear corepressor with conserved domains for RING finger, B boxes, leucine zipper α helical coiled-coil region, plant homeo domain finger, and bromo domain. The plant homeo domain finger and bromo domain of KAP1 cooperatively function as a transcription repression domain by recruiting the histone deacetylase complex NuRD and histone H3 lysine 9-specific methyltransferase SETDB1. Here we report that KAP1 binds the E2F1 transcription factor in a retinoblastoma protein (pRb)-independent fashion and inhibits E2F1 activity. KAP1 stimulates formation of E2F1-HDAC1 complex and inhibits E2F1 acetylation. Ectopic expression of KAP1 represses E2F1 transcription and apoptosis functions independent of pRb. Depletion of endogenous KAP1 in pRb-deficient Saos2 cells by RNA interference increases E2F1 acetylation level, stimulates E2F1 transcriptional activity, and sensitizes apoptosis response to DNA damage. Therefore, KAP1 contributes to the negative regulation of E2F1 and may serve as a partial backup to prevent E2F1-mediated apoptosis in the absence of pRb. |
| doi_str_mv | 10.1074/jbc.M704757200 |
| format | Article |
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Douglas ; Chen, Jiandong</creator><creatorcontrib>Wang, Chuangui ; Rauscher, Frank J. ; Cress, W. Douglas ; Chen, Jiandong</creatorcontrib><description>KAP1 is a nuclear corepressor with conserved domains for RING finger, B boxes, leucine zipper α helical coiled-coil region, plant homeo domain finger, and bromo domain. The plant homeo domain finger and bromo domain of KAP1 cooperatively function as a transcription repression domain by recruiting the histone deacetylase complex NuRD and histone H3 lysine 9-specific methyltransferase SETDB1. Here we report that KAP1 binds the E2F1 transcription factor in a retinoblastoma protein (pRb)-independent fashion and inhibits E2F1 activity. KAP1 stimulates formation of E2F1-HDAC1 complex and inhibits E2F1 acetylation. Ectopic expression of KAP1 represses E2F1 transcription and apoptosis functions independent of pRb. Depletion of endogenous KAP1 in pRb-deficient Saos2 cells by RNA interference increases E2F1 acetylation level, stimulates E2F1 transcriptional activity, and sensitizes apoptosis response to DNA damage. Therefore, KAP1 contributes to the negative regulation of E2F1 and may serve as a partial backup to prevent E2F1-mediated apoptosis in the absence of pRb.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M704757200</identifier><identifier>PMID: 17704056</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Apoptosis ; Cell Line ; Cell Line, Tumor ; DNA Damage ; DNA-Binding Proteins - metabolism ; DNA-Binding Proteins - physiology ; E2F1 Transcription Factor - metabolism ; E2F1 Transcription Factor - physiology ; Gene Expression Regulation ; Gene Expression Regulation, Neoplastic ; Humans ; Models, Biological ; Models, Genetic ; Protein Binding ; Protein Structure, Tertiary ; Repressor Proteins - metabolism ; Repressor Proteins - physiology ; Retinoblastoma Protein - metabolism ; Transfection ; Tripartite Motif-Containing Protein 28</subject><ispartof>The Journal of biological chemistry, 2007-10, Vol.282 (41), p.29902-29909</ispartof><rights>2007 © 2007 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c532t-12fd1556100cc99b3b7575e39bf2790b9636acacb232efb9e1919d5ea25d4e543</citedby><cites>FETCH-LOGICAL-c532t-12fd1556100cc99b3b7575e39bf2790b9636acacb232efb9e1919d5ea25d4e543</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17704056$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wang, Chuangui</creatorcontrib><creatorcontrib>Rauscher, Frank J.</creatorcontrib><creatorcontrib>Cress, W. Douglas</creatorcontrib><creatorcontrib>Chen, Jiandong</creatorcontrib><title>Regulation of E2F1 Function by the Nuclear Corepressor KAP1</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>KAP1 is a nuclear corepressor with conserved domains for RING finger, B boxes, leucine zipper α helical coiled-coil region, plant homeo domain finger, and bromo domain. The plant homeo domain finger and bromo domain of KAP1 cooperatively function as a transcription repression domain by recruiting the histone deacetylase complex NuRD and histone H3 lysine 9-specific methyltransferase SETDB1. Here we report that KAP1 binds the E2F1 transcription factor in a retinoblastoma protein (pRb)-independent fashion and inhibits E2F1 activity. KAP1 stimulates formation of E2F1-HDAC1 complex and inhibits E2F1 acetylation. Ectopic expression of KAP1 represses E2F1 transcription and apoptosis functions independent of pRb. Depletion of endogenous KAP1 in pRb-deficient Saos2 cells by RNA interference increases E2F1 acetylation level, stimulates E2F1 transcriptional activity, and sensitizes apoptosis response to DNA damage. Therefore, KAP1 contributes to the negative regulation of E2F1 and may serve as a partial backup to prevent E2F1-mediated apoptosis in the absence of pRb.</description><subject>Apoptosis</subject><subject>Cell Line</subject><subject>Cell Line, Tumor</subject><subject>DNA Damage</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>DNA-Binding Proteins - physiology</subject><subject>E2F1 Transcription Factor - metabolism</subject><subject>E2F1 Transcription Factor - physiology</subject><subject>Gene Expression Regulation</subject><subject>Gene Expression Regulation, Neoplastic</subject><subject>Humans</subject><subject>Models, Biological</subject><subject>Models, Genetic</subject><subject>Protein Binding</subject><subject>Protein Structure, Tertiary</subject><subject>Repressor Proteins - metabolism</subject><subject>Repressor Proteins - physiology</subject><subject>Retinoblastoma Protein - metabolism</subject><subject>Transfection</subject><subject>Tripartite Motif-Containing Protein 28</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0E1v1DAQBmALgehSuHKEHBC3LDN2nMTiVK26BVE-BFTiZtnOZNdVdr21E1D_fV2yUk8IH2zJeubV6GXsJcISoaneXVu3_NxA1ciGAzxiC4RWlELir8dsAcCxVFy2J-xZSteQT6XwKTvBJo-ArBfs_XfaTIMZfdgXoS_O-RqL9bR3fz_sbTFuqfgyuYFMLFYh0iFSSiEWn86-4XP2pDdDohfH95Rdrc9_rj6Ul18vPq7OLksnBR9L5H2HUtYI4JxSVti8rCShbM8bBVbVojbOOMsFp94qQoWqk2S47CqSlThlb-fcQww3E6VR73xyNAxmT2FKum6F5BLr_0IOvJFSyAyXM3QxpBSp14fodybeagR936vOveqHXvPAq2PyZHfUPfBjkRm8mcHWb7Z_fCRtfXBb2mnecl2h5koBz-z1zHoTtNlEn_TVDw4oANr7S2TRzoJyo789RZ2cp72jLoe6UXfB_2vJOyl5mHs</recordid><startdate>20071012</startdate><enddate>20071012</enddate><creator>Wang, Chuangui</creator><creator>Rauscher, Frank J.</creator><creator>Cress, W. 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Douglas ; Chen, Jiandong</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c532t-12fd1556100cc99b3b7575e39bf2790b9636acacb232efb9e1919d5ea25d4e543</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Apoptosis</topic><topic>Cell Line</topic><topic>Cell Line, Tumor</topic><topic>DNA Damage</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>DNA-Binding Proteins - physiology</topic><topic>E2F1 Transcription Factor - metabolism</topic><topic>E2F1 Transcription Factor - physiology</topic><topic>Gene Expression Regulation</topic><topic>Gene Expression Regulation, Neoplastic</topic><topic>Humans</topic><topic>Models, Biological</topic><topic>Models, Genetic</topic><topic>Protein Binding</topic><topic>Protein Structure, Tertiary</topic><topic>Repressor Proteins - metabolism</topic><topic>Repressor Proteins - physiology</topic><topic>Retinoblastoma Protein - metabolism</topic><topic>Transfection</topic><topic>Tripartite Motif-Containing Protein 28</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wang, Chuangui</creatorcontrib><creatorcontrib>Rauscher, Frank J.</creatorcontrib><creatorcontrib>Cress, W. Douglas</creatorcontrib><creatorcontrib>Chen, Jiandong</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>Nucleic Acids Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wang, Chuangui</au><au>Rauscher, Frank J.</au><au>Cress, W. Douglas</au><au>Chen, Jiandong</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Regulation of E2F1 Function by the Nuclear Corepressor KAP1</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2007-10-12</date><risdate>2007</risdate><volume>282</volume><issue>41</issue><spage>29902</spage><epage>29909</epage><pages>29902-29909</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>KAP1 is a nuclear corepressor with conserved domains for RING finger, B boxes, leucine zipper α helical coiled-coil region, plant homeo domain finger, and bromo domain. The plant homeo domain finger and bromo domain of KAP1 cooperatively function as a transcription repression domain by recruiting the histone deacetylase complex NuRD and histone H3 lysine 9-specific methyltransferase SETDB1. Here we report that KAP1 binds the E2F1 transcription factor in a retinoblastoma protein (pRb)-independent fashion and inhibits E2F1 activity. KAP1 stimulates formation of E2F1-HDAC1 complex and inhibits E2F1 acetylation. Ectopic expression of KAP1 represses E2F1 transcription and apoptosis functions independent of pRb. Depletion of endogenous KAP1 in pRb-deficient Saos2 cells by RNA interference increases E2F1 acetylation level, stimulates E2F1 transcriptional activity, and sensitizes apoptosis response to DNA damage. Therefore, KAP1 contributes to the negative regulation of E2F1 and may serve as a partial backup to prevent E2F1-mediated apoptosis in the absence of pRb.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>17704056</pmid><doi>10.1074/jbc.M704757200</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; Alma/SFX Local Collection |
| subjects | Apoptosis Cell Line Cell Line, Tumor DNA Damage DNA-Binding Proteins - metabolism DNA-Binding Proteins - physiology E2F1 Transcription Factor - metabolism E2F1 Transcription Factor - physiology Gene Expression Regulation Gene Expression Regulation, Neoplastic Humans Models, Biological Models, Genetic Protein Binding Protein Structure, Tertiary Repressor Proteins - metabolism Repressor Proteins - physiology Retinoblastoma Protein - metabolism Transfection Tripartite Motif-Containing Protein 28 |
| title | Regulation of E2F1 Function by the Nuclear Corepressor KAP1 |
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