| pubmed-article:10611298 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10611298 | lifeskim:mentions | umls-concept:C0271510 | lld:lifeskim |
| pubmed-article:10611298 | lifeskim:mentions | umls-concept:C1336789 | lld:lifeskim |
| pubmed-article:10611298 | lifeskim:mentions | umls-concept:C1334871 | lld:lifeskim |
| pubmed-article:10611298 | lifeskim:mentions | umls-concept:C0205246 | lld:lifeskim |
| pubmed-article:10611298 | lifeskim:mentions | umls-concept:C1704241 | lld:lifeskim |
| pubmed-article:10611298 | lifeskim:mentions | umls-concept:C1533148 | lld:lifeskim |
| pubmed-article:10611298 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:10611298 | pubmed:issue | 26 | lld:pubmed |
| pubmed-article:10611298 | pubmed:dateCreated | 2000-1-27 | lld:pubmed |
| pubmed-article:10611298 | pubmed:abstractText | Hypermethylated in cancer (HIC-1), a new candidate tumor suppressor gene located in 17p13.3, encodes a protein with five C(2)H(2) zinc fingers and an N-terminal broad complex, tramtrack, and bric à brac/poxviruses and zinc-finger (BTB/POZ) domain found in actin binding proteins or transcriptional regulators involved in chromatin modeling. In the human B cell lymphoma (BCL-6) and promyelocityc leukemia (PLZF) oncoproteins, this domain mediates transcriptional repression through its ability to recruit a silencing mediator of retinoid and thyroid hormone receptor (SMRT)/nuclear receptor corepressor (N-CoR)-mSin3A-histone deacetylase (HDAC) complex, a mechanism shared with numerous transcription factors. HIC-1 appears unique because it contains a 13-aa insertion acquired late in evolution, because it is not found in its avian homologue, gammaF1-binding protein isoform B (gammaFBP-B), a transcriptional repressor of the gammaF-crystallin gene. This insertion, located in a conserved region involved in the dimerization and scaffolding of the BTB/POZ domain, mainly affects slightly the ability of the HIC-1 and gammaFBP-B BTB/POZ domains to homo- and heterodimerize in vivo, as shown by mammalian two-hybrid experiments. Both the HIC-1 and gammaFBP-B BTB/POZ domains behave as autonomous transcriptional repression domains. However, in striking contrast with BCL-6 and PLZF, both HIC-1 and gammaFBP-B similarly fail to interact with members of the HDAC complexes (SMRT/N-CoR, mSin3A or HDAC-1) in vivo and in vitro. In addition, a general and specific inhibitor of HDACs, trichostatin A, did not alleviate the HIC-1- and gammaFBP-B-mediated transcriptional repression, as previously shown for BCL-6. Taken together, our studies show that the recruitment onto target promoters of an HDAC complex is not a general property of transcriptional repressors containing a conserved BTB/POZ domain. | lld:pubmed |
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| pubmed-article:10611298 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:10611298 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:10611298 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10611298 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:10611298 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:10611298 | pubmed:author | pubmed-author:LeprinceDD | lld:pubmed |
| pubmed-article:10611298 | pubmed:author | pubmed-author:DeltourSS | lld:pubmed |
| pubmed-article:10611298 | pubmed:author | pubmed-author:GuerardelCC | lld:pubmed |
| pubmed-article:10611298 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10611298 | pubmed:day | 21 | lld:pubmed |
| pubmed-article:10611298 | pubmed:volume | 96 | lld:pubmed |
| pubmed-article:10611298 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10611298 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10611298 | pubmed:pagination | 14831-6 | lld:pubmed |
| pubmed-article:10611298 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
