||Accumulation of ICBP90 in breast-cancer cells might suppress expression of tumor suppressor genes through deacetylation of histones after recruitment of HDAC1. Accumulation of ICBP90 in breast-cancer cells might suppress expression of tumor suppressor genes through deacetylation of histones after recruitment of HDAC1. Androgen receptor, Tip60, and HDAC1 form a trimeric complex upon the endogenous AR-responsive PSA promoter, acetylation and deacetylation of the AR is an important mechanism for regulating transcriptional activity. Che-1 affects cell growth by interfering with the recruitment of HDAC1 by retinoblastoma protein. Che-1 overexpression activates DNA synthesis in quiescent NIH-3T3 cells through HDAC1 displacement. Counterregulation of chromatin deacetylation and histone deacetylase occupancy at the integrated promoter of human immunodeficiency virus type 1 (HIV-1) by the HIV-1 repressor YY1 and HIV-1 activator Tat. Data show that the adenovirus protein Gam1 counteracts histone deacetylase 1 sumoylation both in vivo and in vitro. Expression profile of histone deacetylase 1 in gastric cancer tissues. Ezh2 competes with HDAC1 in binding to pRb2/p130, disrupting their occupancy on the cyclin A promoter. Gfi1 associates with G9a and HDAC1 on the promoter of the cell cycle regulator p21Cip/WAF1, resulting in an increase in K9 dimethylation at histone H3. HDAC-Sin3A complex regulates LHR Gene transcription. HDAC1 has a role in interferon-stimulated transcription and innate antiviral immunity. HDAC1 interacts with p300 C/H3 domain. Its overexpression interferes with either activation of Gal14p300 fusion protein or p300-dependent co-activation of MyoD and p53. E1A competes with HDAC1 for C/H3 binding. HDAC1 is displaced from the p21WAF1/CIP1 promoter by Che-1 in human colonic carcinoma. HDAC1 negatively regulates the cardiovascular transcription factor KLF5 through direct interaction. HDAC1 represses the small GTPase RhoB expression in human nonsmall lung carcinoma cell line. HDAC1 upregulated in pre-malignant and malignant lesions, with the highest increase in expression in hormone refractory (HR) prostate cancer; in CWR22 xenograft model, androgen dependent regulation of HDAC1 demonstrated. Here we show that HDAC1 associates with and blocks Ser133 phosphorylation of CREB during pre-stimulus and attenuation phases of the cAMP response. Histone acetylation and deacetylation, catalyzed by multisubunit complexes, play a key role in the regulation of eukaryotic gene expression. The protein encoded by this gene belongs to the histone deacetylase/acuc/apha family and is a component of the histone deacetylase complex. It also interacts with retinoblastoma tumor-suppressor protein and this complex is a key element in the control of cell proliferation and differentiation. Together with metastasis-associated protein-2, it deacetylates p53 and modulates its effect on cell growth and apoptosis. IkappaBalpha regulates the transcriptional activity of homeodomain-containing proteins positively through cytoplasmic sequestration of HDAC1 and HDAC3. In prostate tissues, the abundance of HDAC1 protein, which was exclusively expressed in the cell nucleus, was similar in normal and malignant epithelial cells, but was usually lower in stromal cells. MeCP2 acts as a corepressor of PU.1 probably due to facilitating complex formation with mSin3A and HDACs. Phosphatase inhibition leads to histone deacetylases 1 and 2 phosphorylation and disruption of corepressor interactions. SENP1's ability to enhance AR-dependent transcription is not mediated through desumoylation of AR, but rather through its ability to deconjugate histone deacetylase 1 (HDAC1), thereby reducing its deacetylase activity. SMAR1 regulates cyclin D1 by modification of chromatin through the SIN3/histone deacetylase 1 complex. Tax interacts directly with HDAC1 and regulates binding of the repressor to the HTLV-1 promoter. The HDAC1 complex binds MDM2 in a p53-independent manner and deacetylates p53 at all known acetylated lysines in vivo. The MLL repression domain specifically interacts with HDAC1. The transcriptional repressor mSin3A associates with histone deacetylase 1 forming a co-repressor complex. See also PMID (PubMed identifier) 9150133. We demonstrate that MI-ER1 repressor activity is due to interaction and recruitment of a trichostatin A-sensitive HDAC1, deletion analysis revealed that recruitment of HDAC1 to hMI-ER1alpha and hMI-ER1beta occurs through their common ELM2 domain. We investigated occupancy of ER-alpha promoter by pRb2/p130-E2F4/5-HDAC1-SUV39 H1-p300 and pRb2/p130-E2F4/5-HDAC1-SUV39H1-DNMT1 complexes, and provided a link between pRb2/p130 and chromatin-modifying enzymes in the regulation of ER-alpha transcription. Associated with silencing DAP kinase gene expression in colorectal and gastric cancers. Association with proliferating cell nuclar antigen, integrating DNA replication and chromatin modification. Deacetylase HDAC1 acts as an antagonist of the tumor suppressor p53 in the regulation of the cyclin-dependent kinase inhibitor p21. Histone deacetylase 1 overexpression is associated with advanced stage esophageal squamous cell carcinoma. Histone deacetylase has a role in transforming growth factor-beta signaling in breast cancer cells. Interaction of HPV type 31 E7 with HDACs and the integrity of the zinc finger-like motifs are essential for extending the life span of keratinocytes and for stable maintenance of viral genomes. Interaction with large subunit of replication factor C. Interaction with mCpG-binding domain of MBD2. Interleukin-5 transcription repression by the glucocorticoid receptor targets GATA3 signaling and involves histone deacetylase recruitment. Localization in Aurora-A-positive centrosomes in M phase. P52 NF-kappaB subunit associates with histone deacetylase 1 when p53 represses cyclin D1 transcription through down regulation of Bcl-3. Plays a critical role in repression of endothelial constitutive nitric oxide synthase gene. Recruited by prohibitin for transcriptional repression. Role in regulation of the telomerase reverse transcriptase (hTERT) gene. Stabilization of NF-E4 by acetylation is PCAF-dependent; acetylation of Lys(43) also reduces the interaction between NF-E4 and HDAC1, potentially maximizing the activating ability of the factor.