Ask about this productRelated genes to: HDAC11 Blocking Peptide
- Gene:
- HDAC11 NIH gene
- Name:
- histone deacetylase 11
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 3p25.1
- Locus Type:
- gene with protein product
- Date approved:
- 2002-08-09
- Date modifiied:
- 2014-11-19
Related products to: HDAC11 Blocking Peptide
Related articles to: HDAC11 Blocking Peptide
- Hepatocellular carcinoma (HCC), a malignancy driven by multifaceted genetic and epigenetic mechanisms, is the leading cause of cancer deaths worldwide. Long non-coding RNAs (lncRNAs), particularly super-enhancer-associated lncRNAs (SE-lncRNAs), have emerged as critical regulators of tumorigenesis. - Source: PubMed
Publication date: 2026/05/13
Ye WeidongXiao JunyuanLi JiaxinYang ChengLi ChunlaiXi ZhifengCheng Zhuoan - Histone deacetylase 11 (HDAC11) is a lysine de-fatty acylase whose cellular substrates and mechanisms remain incompletely defined. Here, using metabolic labeling, mass spectrometry, click chemistry, and standard molecular biology, we show that SF3B2 is modified by lysine myristoylation at K10 and that HDAC11 efficiently removes this modification in cells, establishing SF3B2 as a direct enzymatic substrate. A de-myristoylation mimetic mutant (SF3B2 K10R) exhibits altered pre-mRNA binding activity in a context-dependent manner. In HCC cells, loss of SF3B2 lysine myristoylation enhances SF3B2 association with androgen receptor (AR) splice variant loci and promotes alternative splicing towards the AR-v7 variant. Consistently, HDAC11 overexpression increases, and HDAC11 knockdown decreases, the AR-v7/AR-FL splice isoform ratio in HCC cells in a manner requiring HDAC11 catalytic activity and recapitulated by SF3B2 K10R. In contrast, modulation of HDAC11 does not alter AR splicing in prostate cancer cells, indicating cell type specific regulation. Together, these findings establish lysine myristoylation as a reversible regulatory modification on a spliceosomal component and reveal HDAC11-catalyzed de-myristoylation of SF3B2 as a mechanism that can tune alternative splicing in liver cancer cells. - Source: PubMed
Publication date: 2026/02/23
Clements JennaJung SungCao JiSun LeiGhezzi Ana CarolinaGaylen MitchellReid La'QuanPeng Changmin - Metabolic dysfunction-associated steatotic liver disease (MASLD) is frequently accompanied by hepatic fibrosis and systemic cardiovascular complications; however, the mechanistic interplay between coagulation abnormalities and disease progression remains poorly defined. Here, analyses of liver tissues and plasma from patients with MASLD, together with complementary mouse models, suggest an important role of immunothrombosis in fibrotic progression. In MASLD mouse models, pharmacological anticoagulation with dabigatran or aspirin attenuates fibrosis but increases systemic bleeding risk, highlighting the need for more selective strategies. Mechanistically, neutrophil extracellular traps (NETs) promote localized fibrin deposition within the hepatic microvasculature, leading to impaired microcirculation and liver sinusoidal endothelial cell (LSEC) capillarization associated with increased Piezo1-dependent mechanosensation, thereby exacerbating fibrosis. Further investigation identifies neutrophil-derived fibrinogen-like protein 2 (FGL2) as a key upstream regulator of NETs formation through interaction with histone deacetylase 11 (HDAC11), promoting histone H3 deacetylation and facilitating PAD4-mediated citrullination to drive NETs release. Genetic disruption of FGL2 or NETs inhibition restores LSEC fenestration, improves microvascular hemodynamics, and attenuates fibrosis without increasing systemic bleeding risk. Together, these findings define an immunothrombotic axis linking neutrophil-derived FGL2-HDAC11 signaling to NETs formation and endothelial dysfunction in MASLD, providing mechanistic insight into the interplay between coagulation and metabolic liver disease. - Source: PubMed
Publication date: 2026/05/10
Li XitangHu JunjianHai SupingHu PengWu WenhuiGao QiangYu BinghuiXu FeiyangZheng XizheGuan QiantingXiang HuilingXi DongYan WeimingWang PengZhang Bin-HaoNing QinWang Xiaojing - Idiopathic pulmonary fibrosis (IPF) is a fatal interstitial lung disease where macrophages drive fibrogenesis, yet Hdac11's role is unclear. We first identify pronounced Hdac11 upregulation in IPF lungs, which is associated with an enrichment in alveolar macrophages (AMs). Genetic ablation of Hdac11 or adoptive transfer of Hdac11-deficient macrophages markedly attenuates fibrosis. Specifically, Hdac11 deficiency significantly reduces M2 macrophage polarization in vivo and vitro and is associated with reduced macrophage-myofibroblast transition (MMT) like phenotypic reprogramming, thereby decreasing myofibroblast accumulation and profibrotic gene expression. Mechanistically, impaired mitophagy mediates Hdac11-mediated M2 macrophage polarization and is associated with MMT-like changes. Hdac11 regulates mitochondrial quality control by deacetylating Parkin at lysine 76, promoting its ubiquitination and degradation, which impairs mitophagy and drives profibrotic macrophage activation. Pharmacological Hdac11 inhibition effectively reverses bleomycin-induced fibrosis. Taken together, our work identifies Hdac11 as a target of Parkin-mediated mitophagy in macrophages, establishing Hdac11-Parkin axis disruption as an important mechanism in IPF and highlighting Hdac11 inhibition as a potential therapeutic strategy. - Source: PubMed
Publication date: 2026/04/17
Nie YunjuanXu LiLiu YanyanLi JiaoWang ZhixuZhai XiaorunSun XiaoruHu ChunxiaoXu BoWu YaxianYu HaitaoKarpurapu ManjulaGuo HuaqiChai Gaoshang - Mood stabilizers (MS) are the cornerstone of maintenance treatment for bipolar disorder. However, their mechanisms of action remain only partially understood. Increasing evidence suggests that MS may exert part of their therapeutic effects through epigenetic modulations. In this exploratory study, we investigated the effects of therapeutic concentrations of six MS - valproic acid (VPA), lithium, lamotrigine, risperidone, aripiprazole, and quetiapine - on the expression of 82 genes involved in DNA methylations and histone modifications in HeLa cells. After seven days of exposure, VPA induced the most extensive transcriptional changes, with differential expression of 17 out of 82 genes, predominantly involved in histone modifications (acetylation, methylation, phosphorylation, ubiquitination). Notably, VPA upregulated HDAC1, HDAC2, HDAC9, HDAC11, KDM5B, and PAK1 mRNA levels with fold-changes >1.3. Corresponding increased protein levels were observed only for KDM5B and PAK1. VPA also induced direct inhibition of total HDAC activity, unlike lithium and quetiapine. Lithium and quetiapine upregulated HDAC2 and ESCO1 mRNA levels. Lithium and quetiapine did not modify HDAC2 protein levels. Other MS showed no significant transcriptional effects at day 7. Overall, MS-induced transcriptional changes were mainly restricted to genes involved in histone modifications, with minimal effects on DNA methylation-related genes. These findings suggest that MS, particularly VPA, modulate the transcription of epigenetic machinery genes in HeLa cells. HDAC2 upregulation may represent a shared transcriptional response across several MS, although the absence of consistent protein-level changes warrants caution. These results are exploratory and require replication in more physiologically relevant models to determine their biological and clinical significance. - Source: PubMed
Publication date: 2026/04/08
Hennion VincentRathes ArthnaPuszkiel AlicjaBellivier FrankDecleves XavierFroelicher-Bournaud LéoEtain BrunoMarie-Claire Cynthia