| http://purl.uniprot.org/citations/19505873 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/19505873 | http://www.w3.org/2000/01/rdf-schema#comment | "Transcription factor activating enhancer-binding protein 4 (AP-4) is a basic helix-loop-helix protein that binds to E-box elements. AP-4 has received increasing attention for its regulatory role in cell growth and development, including transcriptional repression of the human homolog of murine double minute 2 (HDM2), an important oncoprotein controlling cell growth and survival, by an unknown mechanism. Here we demonstrate that AP-4 binds to an E-box located in the HDM2-P2 promoter and represses HDM2 transcription in a p53-independent manner. Incremental truncations of AP-4 revealed that the C-terminal Gln/Pro-rich domain was essential for transcriptional repression of HDM2. To further delineate the molecular mechanism(s) of AP-4 transcriptional control and its potential implications, we used DNA-affinity purification followed by complementary quantitative proteomics, cICAT and iTRAQ labeling methods, to identify a previously unknown E-box-bound AP-4 protein complex containing 75 putative components. The two labeling methods complementarily quantified differentially AP-4-enriched proteins, including the most significant recruitment of DNA damage response proteins, followed by transcription factors, transcriptional repressors/corepressors, and histone-modifying proteins. Specific interaction of AP-4 with CCCTC binding factor, stimulatory protein 1, and histone deacetylase 1 (an AP-4 corepressor) was validated using AP-4 truncation mutants. Importantly, inclusion of trichostatin A did not alleviate AP-4-mediated repression of HDM2 transcription, suggesting a previously unidentified histone deacetylase-independent repression mechanism. In contrast, the complementary quantitative proteomics study suggested that transcription repression occurs via coordination of AP-4 with other transcription factors, histone methyltransferases, and/or a nucleosome remodeling SWI.SNF complex. In addition to previously known functions of AP-4, our data suggest that AP-4 participates in a transcriptional-regulating complex at the HDM2-P2 promoter in response to DNA damage."xsd:string |
| http://purl.uniprot.org/citations/19505873 | http://purl.org/dc/terms/identifier | "doi:10.1074/mcp.m900013-mcp200"xsd:string |
| http://purl.uniprot.org/citations/19505873 | http://purl.uniprot.org/core/author | "Chen Y.J."xsd:string |
| http://purl.uniprot.org/citations/19505873 | http://purl.uniprot.org/core/author | "Huang H.H."xsd:string |
| http://purl.uniprot.org/citations/19505873 | http://purl.uniprot.org/core/author | "Wu W.G."xsd:string |
| http://purl.uniprot.org/citations/19505873 | http://purl.uniprot.org/core/author | "Ku W.C."xsd:string |
| http://purl.uniprot.org/citations/19505873 | http://purl.uniprot.org/core/author | "Chen Y.J.'"xsd:string |
| http://purl.uniprot.org/citations/19505873 | http://purl.uniprot.org/core/author | "Chiu S.K."xsd:string |
| http://purl.uniprot.org/citations/19505873 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
| http://purl.uniprot.org/citations/19505873 | http://purl.uniprot.org/core/name | "Mol Cell Proteomics"xsd:string |
| http://purl.uniprot.org/citations/19505873 | http://purl.uniprot.org/core/pages | "2034-2050"xsd:string |
| http://purl.uniprot.org/citations/19505873 | http://purl.uniprot.org/core/title | "Complementary quantitative proteomics reveals that transcription factor AP-4 mediates E-box-dependent complex formation for transcriptional repression of HDM2."xsd:string |
| http://purl.uniprot.org/citations/19505873 | http://purl.uniprot.org/core/volume | "8"xsd:string |
| http://purl.uniprot.org/citations/19505873 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/19505873 |
| http://purl.uniprot.org/citations/19505873 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/19505873 |
| http://purl.uniprot.org/uniprot/P04637#attribution-58A2CFF8E52030E8F7D48FD978C426D8 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/19505873 |
| http://purl.uniprot.org/uniprot/Q01664#attribution-042E52DEF074111DF291E73491A498B3 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/19505873 |
| http://purl.uniprot.org/uniprot/#_Q15554-mappedCitation-19505873 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/19505873 |
| http://purl.uniprot.org/uniprot/#_O15156-mappedCitation-19505873 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/19505873 |
| http://purl.uniprot.org/uniprot/#_O15347-mappedCitation-19505873 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/19505873 |
| http://purl.uniprot.org/uniprot/#_P62826-mappedCitation-19505873 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/19505873 |
| http://purl.uniprot.org/uniprot/#_O95365-mappedCitation-19505873 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/19505873 |
| http://purl.uniprot.org/uniprot/#_Q12800-mappedCitation-19505873 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/19505873 |
| http://purl.uniprot.org/uniprot/#_Q12824-mappedCitation-19505873 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/19505873 |