Ask about this productRelated genes to: SIN3A antibody
- Gene:
- SIN3A NIH gene
- Name:
- SIN3 transcription regulator family member A
- Previous symbol:
- -
- Synonyms:
- KIAA0700, DKFZP434K2235
- Chromosome:
- 15q24.2
- Locus Type:
- gene with protein product
- Date approved:
- 2002-10-09
- Date modifiied:
- 2016-10-05
Related products to: SIN3A antibody
Related articles to: SIN3A antibody
- Despite antiretroviral therapy, human immunodeficiency virus type 1 (HIV-1) persists in latently-infected cells through epigenetic and transcriptional mechanisms. Latency-reversing agents have failed clinically, partly due to incomplete understanding of HIV-1 latency reversal. Here, using DNA-affinity capture and mass spectrometry on the HIV-1 5' long terminal repeat (5'LTR) enhancer-core promoter, we identify KLF16 (Krüppel-like Factor 16) as a novel regulator of HIV-1 gene expression. KLF16 binds to the HIV-1 5'LTR at Sp1 binding sites, and KLF16 depletion reactivates latent HIV-1 in T-lymphoid and monocytic cell models. Mechanistically, KLF16 represses HIV-1 transcription by competing with Sp1 for promoter binding and by recruiting the Sin3A/HDAC1 and HP1α/Suv39H1 repressive epigenetic complexes. KLF16 is also upregulated in CD4 T cells from ART-treated people with HIV-1 upon T-cell activation. Additionally, All-Trans retinoic acid (ATRA) reactivates latent HIV-1 in myeloid cells, partly by downregulating KLF16. These findings establish KLF16 as a novel transcriptional repressor of HIV-1, identifying it as a potential promising therapeutic target for cure strategies. - Source: PubMed
Publication date: 2026/05/04
Santangelo MarionBendoumou MaryamDutilleul AntoineKhalfi SoumiaPlant EstelleNgassaki-Yoka Christ DominiquePilosio LisaVanhulle CarolineDias JonathanMarray TristanFattaccioli AntoineDieu MarcRouty Jean-PierreRohr OlivierRenard PatriciaAncuta PetronelaVan Lint Carine - Human RNA polymerase II (Pol II) regulates transcription of significant number of snRNA and proliferation-related mRNA genes by involving Little Elongation Complex (LEC) and Super Elongation Complex (SEC) respectively. However, underlying mechanisms of these differential involvements of Pol II are not known. In this study, we show that human ELL, through its dynamic differential association within LEC and SEC, controls expression of target snRNA and proliferation-related mRNA genes by regulating Pol II recruitment. Mechanistically, we show that p300-mediated acetylation of Lysine 355 (K355) residue favors ELL monomerization and corresponding ELL•SEC formation and proliferation-related mRNA transcription; and reciprocally, HDAC1-mediated deacetylation favors dimerization and subsequent ELL●LEC formation and snRNA transcription; and vice versa. Physiologically, we show that whereas, mitogen treatment enhances AKT signaling-dependent p300-mediated ELL(K355) acetylation leading to increased ELL●SEC assembly and corresponding proliferation-related mRNA transcription, genotoxic stress causes ATM-mediated ELL phosphorylation-dependent deacetylation of ELL(K355) by Sin3A●HDAC1 complex causing enhanced ELL●LEC assembly and snRNA transcription. - Source: PubMed
Publication date: 2026/04/27
Nandy ArijitDalui SambitTalukdar PrathamaChakraborty PoushaliBhagat GauravMinhas Ekjot KaurRoy SrerupaLahiri AbhishakeBasrur VenkateshaBiswas Debabrata - FAM60A (also known as SINHCAF) is a subunit of the Sin3/HDAC histone deacetylase complex with established roles in chromatin remodeling, yet its broader cellular functions remain largely undefined. Using immunological, biochemical, CRISPR/Cas9, genomic, and proteomic approaches, we mapped the FAM60A interaction network and its functional impact. We reveal that FAM60A binds directly to HDAC1 to recruit Sin3/HDAC, while a dual-domain architecture mediates additional associations with RNA and DNA-binding proteins. CRISPR/Cas9-mediated HDAC1 knockout abolishes the FAM60A-SIN3A interaction, confirming this dependency. Loss of FAM60A triggers widespread transcriptional rewiring, including downregulation of WWC3-a scaffold for LATS1/2 activation. Consequently, YAP1 dephosphorylation and nuclear accumulation shifted cell-cycle dynamics toward G₁ enrichment and conferred resistance to metabolic stress. Restoration of FAM60A or exogenous WWC3 reactivated Hippo "off" signaling, normalized cell-cycle distribution, and reversed stress resistance. These findings establish FAM60A as a pivotal epigenetic tuner linking histone deacetylation to Hippo pathway regulation and nominate the FAM60A-HDAC1-WWC3 axis as a potential therapeutic target to restore growth control in YAP-driven cancers. - Source: PubMed
Publication date: 2026/04/27
Miah MojnuHuda Md NazmulIslam Md RafikulGerald DayebgadohKhator SnehaSaha AkashAlam JahangirThornton Janet LGies AllenBauer Michael AStephens Kimberly ENagalo Bolni MRahman Mohammad AWashburn Michael PMiah Sayem - Histone Deacetylase (HDAC) 1 and 2 are key enzymatic components in multiple large chromatin remodeling complexes including NuRD, SIN3, and CoREST. In addition, both HDAC 1 and 2 contain a large intrinsically disordered region (IDR) within their C-terminal domain (CTD). How HDAC1/2 assemble into these complexes and the structure of the CTD IDR remains poorly understood. Here, we used HDAC1/2 to isolate their protein interaction networks from cells and used crosslinking mass spectrometry (XL-MS) coupled with the Integrative Modeling Platform to build structural models of the NuRD, SIN3A, and CoREST complexes. Next, we implemented an AlphaFold-enabled XL-MS constrained modeling approach to investigate how HDAC1 could assemble into these complexes. We show that the CTD IDR of HDAC1 folds into alpha helices in these complexes. Finally, we built a complete integrative structural model of a NuRD subcomplex including the abundant HDAC1:MBD3:MTA1:GATAD2B:RBBP4 subunits, which included 6 IDRs. The approaches used herein are broadly applicable for the study of protein complexes and protein interaction networks that can provide important insights into IDRs. - Source: PubMed
Publication date: 2026/03/25
Nde JulesMajila KartikZimmermann Rosalyn CKempf CassandraZhang YingCesare JosephThornton Janet LWorkman Jerry LFlorens LaurenceViswanath ShruthiWashburn Michael P - Precise transcriptional regulation is critical for cellular function and development, yet the mechanism of this process remains poorly understood for many genes. To gain a deeper understanding of the regulation of neuropsychiatric disease risk genes, we identify a total of 39 functional enhancers for four dosage-sensitive genes, APP, FMR1, MECP2, and SIN3A, using CRISPR tiling deletion screening in human induced pluripotent stem cell (iPSC)-induced excitatory neurons. More importantly, we discover that allelic enhancer deletions at SIN3A could be compensated by increased transcriptional activities from the other intact allele. Such allelic compensation effects (ACE) on transcription are stably maintained during differentiation and, once established, cannot be reversed by ectopic SIN3A expression. Further, ACE at SIN3A occurs through dosage sensing by the promoter. Together, our findings unravel a regulatory compensation mechanism that ensures stable and precise transcriptional output for SIN3A, and potentially other dosage-sensitive genes. - Source: PubMed
Publication date: 2026/03/25
Ren XingjieZheng LinaLiu YuxiMaliskova LenkaTam Tsz WaiSun YifanLiu HongjiangCui XiekuiLee JerryTakagi Maya AsamiLi BinRen BingWang WeiShen Yin