Ask about this productRelated genes to: MYST2 antibody
- Gene:
- KAT7 NIH gene
- Name:
- lysine acetyltransferase 7
- Previous symbol:
- MYST2
- Synonyms:
- HBOA, HBO1, ZC2HC7
- Chromosome:
- 17q21.33
- Locus Type:
- gene with protein product
- Date approved:
- 2003-06-03
- Date modifiied:
- 2016-10-05
Related products to: MYST2 antibody
Related articles to: MYST2 antibody
- Peripheral hormonal dysfunction is associated with multiple neurological disorders, yet how astrocytes sense circulating stress-related hormones to influence depression pathogenesis remains incompletely understood. Here, we showed that disruption of secretin receptor (SCTR) signaling in dorsal raphe nucleus (DRN) astrocytes promotes depression-like behaviors. We identified AMPKα1 as a key downstream effector of astrocytic SCTR signaling and demonstrate its role in regulating astrocytic secretion of metallothionein-1 (Mt1) and downstream megalin-mediated AMPKα2 signaling in serotonergic neurons. We further identified the transcription factor Foxc2 as a downstream target of neuronal AMPKα2 that modulates depressive-like behaviors through suppression of serotonergic activity and reduced neuronal excitability. Mechanistically, AMPKα2 regulates phosphorylation of the acetyltransferase KAT7, thereby modulating histone H4 acetylation and Foxc2 transcription. Together, these findings delineate an astrocyte-neuron signaling axis linking SCTR-AMPKα1 signaling in astrocytes to epigenetic regulation of Foxc2 by AMPKα2-KAT7/H4ac signaling in serotonergic neurons, providing fundamental insight into circuit-level mechanisms underlying depression. - Source: PubMed
Publication date: 2026/09/27
Meng FantaoLiu JingDai JuanjuanWu MinWang WentaoZhang MengdiJiang ShujunCao YifanXu LihongDu LinWang DanZhao DiQin GaofengWang DongLi WeiLi Chen - Lysine acetyltransferase 7 (KAT7), also known as HBO1 or MYST2, is highly expressed in multiple cancers. This study aims to explore the expression patterns of KAT7 in breast cancer and its impact on phenotypes of breast cancer cells. - Source: PubMed
Publication date: 2026/09/03
Du WeiXiao XiaoyuZhang JiaxinShi ZhongxinYang Minlan - Glioblastoma multiforme (GBM), the most lethal type of primary brain tumor, exhibits profound metabolic plasticity driven by glioma stem cells (GSCs), which sustain therapeutic resistance and tumor recurrence. Here, we elucidate a novel epigenetic-metabolic axis mediated by the histone acetyltransferase KAT7 that orchestrates oxidative phosphorylation (OXPHOS) dominance in GSCs. Through a multi-omics analysis, we demonstrated that KAT7 is preferentially upregulated in GBM, particularly in the classical subtype and in GSC-enriched populations, where it activates Rac family samll GTPase 2 (RAC2) expression via H3K14 acetylation of its promoter. Mechanistically, KAT7-mediated RAC2 upregulation triggers PAK1/2/3 phosphorylation, increasing tricarboxylic acid cycle (TCA) and ATP production. Genetic ablation of KAT7 impairs GSCs self-renewal, induces apoptosis, and suppresses tumor growth in orthotopic xenograft models. Conversely, KAT7 overexpression or pharmacological activation of the KAT7-RAC2 axis restores metabolic fitness and malignant phenotypes. Notably, the small-molecule inhibitor WM-3835, which targets KAT7, exhibits potent anti-GBM efficacy by disrupting H3K14ac and mitochondrial respiration, leading to prolonged survival in mice. Our study identifies KAT7 as a master regulator of GSCs metabolism, revealing an actionable therapeutic target in GBM progression. Targeting the KAT7-RAC2-PAK axis may represent a precise strategy to overcome metabolic plasticity-driven therapeutic resistance in this recalcitrant malignancy. - Source: PubMed
Publication date: 2026/09/08
Liu JilongSun YanfeiZhu YuehuaMu GuangjingWang JiazhengWang LiangliangZhao FeihuZhao ZhiminWang JianHe YingJiang ZhengLi XingangHan MingzhiHuang Bin - The INhibitor of Growth (ING) proteins are plant homeodomain (PHD) zinc-finger epigenetic readers that recognize trimethylated lysine 4 of histone H3 (H3K4me3) and couple it to lysine-acetyltransferase (KAT) or -deacetylase (KDAC) activity on chromatin. ING4 and ING5 are among the family's closest paralogs, which share a four-domain architecture and high sequence identity, with divergence concentrated outside the PHD finger. Earlier reviews focused either on the family as a whole or on the individual INGs. This paper is the first to directly compare ING4 and ING5, including their structures, functions within KAT complexes, and roles in cancer and development, noting where they overlap and diverge. Either paralog can occupy the ING position in HBO1 (KAT7) complexes, whereas only ING5 is found in MOZ and MORF (KAT6A/B) complexes. In cancers, ING4 and ING5 generally act as tumor suppressors but can also promote malignancy and stemness. The bulk of evidence for mechanistically explaining the effects of ING4/5 in cancers comes from ectopic overexpression studies. In differentiation, ING5 has been investigated far more than ING4, and the roles of the two mostly diverge: ING5 participates in maintaining stemness in neural, epidermal, and brain tumor initiating cell lines, as well as proliferation of mesenchymal stem cells, whereas ING4 was found to restrain hematopoietic stem cell self-renewal, promote prostate epithelial differentiation, but promote stemness of renal cell carcinoma cells. They nonetheless compensate for one another in embryonic survival, since either paralog alone prevents the arrest seen in double knockouts. The key remaining questions include what determines the structural basis of ING5's MOZ/MORF selectivity, what the precise conditions are under which they substitute for one another, how exactly ING4 and ING5 can be targeted in cancer therapy, and whether the roles of the two paralogs are conserved across species. - Source: PubMed
Publication date: 2026/07/27
Dadoyan SergeyBartizal Tom JAmarsingha SakunikaRiabowol Karl - Pelvic organ prolapse (POP) is a common gynecological disorder severely affecting quality of life, characterized by extracellular matrix (ECM) disruption and metabolic dysregulation. Lactylation is a lactate-induced post-translational modification that regulates gene expression, but its role in POP remains unclear. Here, we demonstrate that enhanced glycolysis and lactate accumulation drive histone lactylation, which impairs mitochondrial function and collagen biosynthesis in POP. Furthermore, we identify histone acetyltransferase Kat7 as a key lactyltransferase that catalyzes H3K14 and H3K18 lactylation via its glutamate residue E508. Notably, H3K14la/H3K18la suppresses the expression of Slc25a51, a mitochondrial NAD transporter, leading to NAD deficiency, hyperacetylation of P5CS, proline depletion, and inhibition of fibroblast proliferation. In vivo, inhibition of glycolysis or Kat7 activity ameliorates vaginal distension-induced lactylation, restores Slc25a51 expression, and improves collagen deposition. Taken together, these findings reveal that histone lactylation disrupts mitochondrial NAD homeostasis and proline metabolism in fibroblasts, thus inhibiting collagen synthesis and enhancing POP pathogenesis. We show that histone H3 lactylation at K14 and K18 promotes POP progression. Kat7 catalyzes lactylation of histone H3 at K14 and K18, and this modification represses Slc25a51 expression, disrupts mitochondrial NAD transport, and inhibits proline-dependent collagen synthesis. Targeting lactate production or Kat7 may restore mitochondrial function and ECM homeostasis, providing a potential treatment for POP. - Source: PubMed
Publication date: 2026/07/23
He YongLiu ChengLi BingshuHong ShashaTang JianmingHuang GuotaoYang LianChen MaoZhang ShufeiXiao YaLiu JianfengNing MinqiJiang NuoXiang ChunrongHuang ShouqiHong Li