KAT5 Antibody
- Known as:
- KAT5 Antibody
- Catalog number:
- aut-7339
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Zyagen
- Gene target:
- KAT5 Antibody
Related genes to: KAT5 Antibody
- Gene:
- KAT5 NIH gene
- Name:
- lysine acetyltransferase 5
- Previous symbol:
- HTATIP
- Synonyms:
- TIP60, PLIP, cPLA2, HTATIP1, ESA1, ZC2HC5
- Chromosome:
- 11q13.1
- Locus Type:
- gene with protein product
- Date approved:
- 2000-04-13
- Date modifiied:
- 2016-10-05
Related products to: KAT5 Antibody
Related articles to: KAT5 Antibody
- The ubiquitin signaling cascade plays a pivotal role in multiple cancer types, yet its role in melanoma progression remains incompletely elucidated. An unbiased and systematic analysis indicates that Ubiquitin-specific peptidase 10 (USP10), a member of USP gene family, was top priority prognostic signature for primary and metastatic melanoma progression-free survival and silencing USP10 markedly impairs the growth and metastatic potential of melanoma cells. We further uncover Forkhead box M1 (FOXM1) as a novel substrate of USP10. USP10 directly binds to FOXM1 and removes ubiquitin chains, thereby enhancing FOXM1 protein stability and driving melanoma progression. Notably, the lysine acetyltransferase KAT5 acetylates FOXM1 at residues K422 and K440, which strengthens the interaction between FOXM1 and USP10, facilitating deubiquitination and subsequent stabilization of FOXM1. Additionally, loss of either USP10 or FOXM1 suppresses the expression of the downstream target Telomerase reverse transcriptase (TERT), triggering cellular senescence. Importantly, we identify Golvatinib, as a novel inhibitor of USP10 that effectively curbs melanoma malignancy in both cellular and animal models. Taken together, these findings highlight the pro-tumorigenic role of USP10 in melanoma and suggest that disrupting the USP10/FOXM1 signaling axis could represent a viable therapeutic approach for treating this aggressive cancer. - Source: PubMed
Publication date: 2026/09/10
Qiu ZhiyuanSun ChenglianWang JuanLiang DapengWang ShangTian LiliDu TongdeHan Chuanchun - Immunotherapy has shown promising efficacy in esophageal squamous cell carcinoma (ESCC), yet its clinical benefits remain limited due to immune evasion. Lactate accumulation in the tumor microenvironment has been found to facilitate immune evasion through protein lactylation. However, the key lactylated substrates and mechanisms driving immune evasion remain undefined. Here, we show that HSPA1A lactylation at lysine 108 (K108) by KAT5 drives CD8⁺ T cell dysfunction and immunotherapy resistance via the STAT1/PD-L1 axis in ESCC. Mechanistically, K108 lactylation enhances HSPA1A binding to STAT1, protecting STAT1 from TRIM25-mediated ubiquitination and proteasomal degradation. This stabilization promotes STAT1 phosphorylation and nuclear translocation, leading to transcriptional upregulation of PD-L1 and subsequent immune evasion. Collectively, these findings highlight the pivotal role of HSPA1A lactylation in facilitating immune evasion via the STAT1/PD-L1 axis, suggesting a potential target for improving immunotherapy efficacy in ESCC. - Source: PubMed
Publication date: 2026/09/24
Wang ZiyiLi XinyanLuo PengLi SuXu YanLi WenyaLiu QuanxingChen YuqiongSun Xiangyu - Rapid repair of genotoxic therapy induced DNA damage mediates treatment resistance in glioblastoma (GBM). The role of non-malignant cell types in the tumor microenvironment in accelerating DNA repair in neoplastic cells is poorly understood. Using spatial transcriptomics, immunofluorescence, metabolomics, patient tissues and preclinical models, we show that tumor associated macrophages (TAMs) in GBM promote DNA repair and treatment resistance in neoplastic cells through the secretion of acetylated amino acids. These acetylated amino acids are consumed by GBM cells, leading to enhanced acetyl Co-A levels, histone acetylation and nucleotide synthesis. Interrupting histone acetylation via inhibition of the acetyltransferase KAT5 breaks these metabolic links and reverses the protective capacity of microenvironment-derived acetylated amino acids and TAMs. Blocking the exchange of acetylated amino acids and their downstream effects is a potential strategy for the treatment of GBM. - Source: PubMed
Publication date: 2026/09/18
Sravya PalavalasaAltay Leyla NurcihanDo KathyFreeman JackGokul AditriLiang NingningScott Andrew JXu JieKorimerla NavyatejaLin AngelicaWang HengWilder-Romans KariSinger AvaO'Brien AlexandraAnimasahun OlamideMeghdadi BaharanBaker EmilyPeterson Erik RMcCulla Elizabeth CZhu ZiqingThomas DafyddAndren AnthonyWong HarrisonSajjakulnukit PeterZhang LiShankar SunitaRavikumar VisweswaranLee Zheng HongCarrion Joseph A NietoBhadury SagnikMiller C RyanSarkaria Jann NHeth Jason AHuse Jason TCamelo-Piragua SandraMorgan Meredith ALawrence Theodore SRao ArvindLyssiotis CostasAl-Holou WajdNagrath DeepakZhou WeihuaWahl Daniel R - Abnormal epigenetic modifications are involved in central nervous system (CNS) diseases. Histones play a crucial role in chromatin structure and function, whose post-translational modifications significantly impact gene expression and chromatin dynamics. Histone acetylation, governed by the balance between histone acetyltransferases (HATs) and histone deacetylases (HDACs), is one of the key modulators of chromatin accessibility and transcriptional activity. Lysine acetyltransferase 5 (KAT5, aka TIP60), a member of the MYST subfamily of HATs, is involved in many cellular processes, including DNA repair, apoptosis, and cell cycle control. Notably, the dysfunction of KAT5 has been implicated in several CNS diseases. In this review, we explored the roles of KAT5 in CNS pathophysiology, emphasizing its involvement in neurological disorders and its potential as a therapeutic target. This review sheds light on the epigenetic mechanisms in CNS diseases mediated by KAT5 and provides valuable information for potential treatment strategies. - Source: PubMed
Publication date: 2026/09/03
Xin XiaomingWu LingjuanLiu MeichenLiu TianYuan ZihanZhang LiangDuan TongqingZhang LeiZhu Xianmin - Inflammation is a pivotal driver of the progression from metabolic dysfunction-associated steatotic liver disease (MASLD) to metabolic dysfunction-associated steatohepatitis (MASH), an aggressive form associated with substantial liver-related mortality. However, the molecular mechanisms underlying the initiation and persistence of liver inflammation remain poorly defined. Here, we demonstrated a previously unrecognized role for hepatic acetyl-CoA synthetase short-chain family member 2 (ACSS2) in MASH, showing that ACSS2 upregulation in patients exacerbates MASH progression by functioning as an epigenetic regulator, independent of its canonical lipogenic role. Mechanistically, ACSS2, in complex with lysine acetyltransferase 5 (KAT5), upregulates allograft inflammatory factor-1 (AIF1) transcription via histone crotonylation, thereby inducing liver inflammation and subsequently resulting in the aberrant accumulation of senescent hepatocytes, which further enhances proinflammatory cytokine production. This ultimately initiates a vicious cycle of chronic inflammation, which directly promotes the progression from simple steatosis to MASH. Thus, our work reveals a mechanistically defined and pivotal role for ACSS2 in promoting the MASLD-to-MASH transition, highlighting its potential as a compelling therapeutic target. - Source: PubMed
Publication date: 2026/07/25
Wen XiaoWu KeyanWang MengyaoMa ZihanWang TaoZhang JingWang BeiChen SiyuanWang JingyiChen SiyueYang FanLiu ChuweiChen XianyangDeng LuCheng YafanMiao Qing RobertSun BaofaRuan XiongzhongLi KaiDuan YajunHu Wenquan