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A Mechanism of COOH–Terminal Binding Protein–Mediated Repression
The E2F4 and E2F5 proteins specifically associate with the Rb-related p130 protein in quiescent cells to repress transcription of various genes encoding proteins important for cell growth. A series of reports has provided evidence that Rb-mediated repression involves both histone deacetylase (HDAC)–...
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| Published in: | Molecular cancer research 2005-10, Vol.3 (10), p.575-583 |
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| Main Authors: | , , , |
| Format: | Article |
| Language: | English |
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| cited_by | cdi_FETCH-LOGICAL-c386t-6c9f9da0fbc87d6880aa6b761da3a10a6eaa3c4be3f5992e0a532faa47a5c65b3 |
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| cites | cdi_FETCH-LOGICAL-c386t-6c9f9da0fbc87d6880aa6b761da3a10a6eaa3c4be3f5992e0a532faa47a5c65b3 |
| container_end_page | 583 |
| container_issue | 10 |
| container_start_page | 575 |
| container_title | Molecular cancer research |
| container_volume | 3 |
| creator | Meloni, Alison R Lai, Chun-Hsiang Yao, Tso-Pang Nevins, Joseph R |
| description | The E2F4 and E2F5 proteins specifically associate with the Rb-related p130 protein in quiescent cells to repress transcription
of various genes encoding proteins important for cell growth. A series of reports has provided evidence that Rb-mediated repression
involves both histone deacetylase (HDAC)–dependent and HDAC-independent events. Our previous results suggest that one such
mechanism for Rb-mediated repression, independent of recruitment of HDAC, involves the recruitment of the COOH-terminal binding
protein (CtBP) corepressor, a protein now recognized to play a widespread role in transcriptional repression. We now find
that CtBP can interact with the histone acetyltransferase, cyclic AMP–responsive element–binding protein (CREB) binding protein,
and inhibit its ability to acetylate histone. This inhibition is dependent on a NH 2 -terminal region of CtBP that is also required for transcription repression. These results thus suggest two complementary
mechanisms for E2F/p130-mediated repression that have in common the control of histone acetylation at target promoters. |
| doi_str_mv | 10.1158/1541-7786.MCR-05-0088 |
| format | article |
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of various genes encoding proteins important for cell growth. A series of reports has provided evidence that Rb-mediated repression
involves both histone deacetylase (HDAC)–dependent and HDAC-independent events. Our previous results suggest that one such
mechanism for Rb-mediated repression, independent of recruitment of HDAC, involves the recruitment of the COOH-terminal binding
protein (CtBP) corepressor, a protein now recognized to play a widespread role in transcriptional repression. We now find
that CtBP can interact with the histone acetyltransferase, cyclic AMP–responsive element–binding protein (CREB) binding protein,
and inhibit its ability to acetylate histone. This inhibition is dependent on a NH 2 -terminal region of CtBP that is also required for transcription repression. These results thus suggest two complementary
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of various genes encoding proteins important for cell growth. A series of reports has provided evidence that Rb-mediated repression
involves both histone deacetylase (HDAC)–dependent and HDAC-independent events. Our previous results suggest that one such
mechanism for Rb-mediated repression, independent of recruitment of HDAC, involves the recruitment of the COOH-terminal binding
protein (CtBP) corepressor, a protein now recognized to play a widespread role in transcriptional repression. We now find
that CtBP can interact with the histone acetyltransferase, cyclic AMP–responsive element–binding protein (CREB) binding protein,
and inhibit its ability to acetylate histone. This inhibition is dependent on a NH 2 -terminal region of CtBP that is also required for transcription repression. These results thus suggest two complementary
mechanisms for E2F/p130-mediated repression that have in common the control of histone acetylation at target promoters.</description><subject>Alcohol Oxidoreductases</subject><subject>Animals</subject><subject>Cells, Cultured</subject><subject>CREB-Binding Protein - metabolism</subject><subject>CtBP</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>E2F Transcription Factors - metabolism</subject><subject>E2F-Rb</subject><subject>histone acetylation</subject><subject>Histone Deacetylases - metabolism</subject><subject>Humans</subject><subject>Phosphoproteins - metabolism</subject><subject>Repressor Proteins - metabolism</subject><subject>transcription</subject><subject>Transcription Factors - metabolism</subject><subject>Transcription, Genetic</subject><subject>Transfection</subject><issn>1541-7786</issn><issn>1557-3125</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><recordid>eNpFkMtOwzAQRS0EouXxCaCsYJVix_UjyxIeRWpVVJW1NXEmrVGTFLsVYsc_8Id8CYlaidWMdM-dkQ4hV4wOGBP6jokhi5XScjDN5jEVMaVaH5E-E0LFnCXiuNsPTI-chfBOaUKZkqekx2TSRinrk4dRNEW7gtqFKmrKKJvNxr_fPwv0lathHd27unD1Mnr1zRZd3UZTLBxssYjmuPEYgmvqC3JSwjrg5WGek7enx0U2jiez55dsNIkt13IbS5uWaQG0zK1WhdSaAshcSVYAB0ZBIgC3wxx5KdI0QQqCJyXAUIGwUuT8nNzs725887HDsDWVCxbXa6ix2QUjteIy4bIFxR60vgnBY2k23lXgvwyjptNnOjWmU2NafYYK0-lre9eHB7u8wuK_dfDVArd7YOWWq0_n0VioLfpWBIK3K8O7D0IJ_gc1T3sy</recordid><startdate>20051001</startdate><enddate>20051001</enddate><creator>Meloni, Alison R</creator><creator>Lai, Chun-Hsiang</creator><creator>Yao, Tso-Pang</creator><creator>Nevins, Joseph R</creator><general>American Association for Cancer Research</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>7X8</scope></search><sort><creationdate>20051001</creationdate><title>A Mechanism of COOH–Terminal Binding Protein–Mediated Repression</title><author>Meloni, Alison R ; Lai, Chun-Hsiang ; Yao, Tso-Pang ; Nevins, Joseph R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c386t-6c9f9da0fbc87d6880aa6b761da3a10a6eaa3c4be3f5992e0a532faa47a5c65b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Alcohol Oxidoreductases</topic><topic>Animals</topic><topic>Cells, Cultured</topic><topic>CREB-Binding Protein - metabolism</topic><topic>CtBP</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>E2F Transcription Factors - metabolism</topic><topic>E2F-Rb</topic><topic>histone acetylation</topic><topic>Histone Deacetylases - metabolism</topic><topic>Humans</topic><topic>Phosphoproteins - metabolism</topic><topic>Repressor Proteins - metabolism</topic><topic>transcription</topic><topic>Transcription Factors - metabolism</topic><topic>Transcription, Genetic</topic><topic>Transfection</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Meloni, Alison R</creatorcontrib><creatorcontrib>Lai, Chun-Hsiang</creatorcontrib><creatorcontrib>Yao, Tso-Pang</creatorcontrib><creatorcontrib>Nevins, Joseph R</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular cancer research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Meloni, Alison R</au><au>Lai, Chun-Hsiang</au><au>Yao, Tso-Pang</au><au>Nevins, Joseph R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A Mechanism of COOH–Terminal Binding Protein–Mediated Repression</atitle><jtitle>Molecular cancer research</jtitle><addtitle>Mol Cancer Res</addtitle><date>2005-10-01</date><risdate>2005</risdate><volume>3</volume><issue>10</issue><spage>575</spage><epage>583</epage><pages>575-583</pages><issn>1541-7786</issn><eissn>1557-3125</eissn><abstract>The E2F4 and E2F5 proteins specifically associate with the Rb-related p130 protein in quiescent cells to repress transcription
of various genes encoding proteins important for cell growth. A series of reports has provided evidence that Rb-mediated repression
involves both histone deacetylase (HDAC)–dependent and HDAC-independent events. Our previous results suggest that one such
mechanism for Rb-mediated repression, independent of recruitment of HDAC, involves the recruitment of the COOH-terminal binding
protein (CtBP) corepressor, a protein now recognized to play a widespread role in transcriptional repression. We now find
that CtBP can interact with the histone acetyltransferase, cyclic AMP–responsive element–binding protein (CREB) binding protein,
and inhibit its ability to acetylate histone. This inhibition is dependent on a NH 2 -terminal region of CtBP that is also required for transcription repression. These results thus suggest two complementary
mechanisms for E2F/p130-mediated repression that have in common the control of histone acetylation at target promoters.</abstract><cop>United States</cop><pub>American Association for Cancer Research</pub><pmid>16254191</pmid><doi>10.1158/1541-7786.MCR-05-0088</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Molecular cancer research, 2005-10, Vol.3 (10), p.575-583 |
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| language | eng |
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| source | EZB Electronic Journals Library |
| subjects | Alcohol Oxidoreductases Animals Cells, Cultured CREB-Binding Protein - metabolism CtBP DNA-Binding Proteins - metabolism E2F Transcription Factors - metabolism E2F-Rb histone acetylation Histone Deacetylases - metabolism Humans Phosphoproteins - metabolism Repressor Proteins - metabolism transcription Transcription Factors - metabolism Transcription, Genetic Transfection |
| title | A Mechanism of COOH–Terminal Binding Protein–Mediated Repression |
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