Ask about this productRelated genes to: RAC3 antibody
- Gene:
- NCOA3 NIH gene
- Name:
- nuclear receptor coactivator 3
- Previous symbol:
- -
- Synonyms:
- RAC3, AIB1, ACTR, p/CIP, TRAM-1, CAGH16, TNRC16, KAT13B, bHLHe42, SRC-3, SRC3
- Chromosome:
- 20q13.12
- Locus Type:
- gene with protein product
- Date approved:
- 1999-12-17
- Date modifiied:
- 2016-10-05
- Gene:
- RAC3 NIH gene
- Name:
- Rac family small GTPase 3
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 17q25.3
- Locus Type:
- gene with protein product
- Date approved:
- 1997-07-11
- Date modifiied:
- 2019-04-16
Related products to: RAC3 antibody
Related articles to: RAC3 antibody
- Nuclear receptor coactivator 3 (NCOA3) is associated with various cancers, but its function and mechanism in glioblastoma multiforme (GBM) are still unclear. Bioinformatics analysis, in vitro cell experiments (NCOA3 silencing (si-NCOA3) or NCOA3 small-molecule inhibitor SI-2), in vivo animal models, and metabolic level detection were used to elucidate the activity of NCOA3 in GBM. The data revealed that GBM tissues had NCOA3 overexpression, which was linked with poor prognosis. It regulates pathways related to glycolysis, the cell cycle, and immunosuppression. Functionally, si-NCOA3/SI-2 suppressed GBM cell proliferation and migration. In vivo, sh-NCOA3/SI-2 demonstrated anti-glioma effects. Metabolically, treatment with si-NCOA3/SI-2 reduced glucose uptake, pyruvate and lactate production, ATP levels, and glycolysis-related enzyme expression in GBM cells. Combination therapy with SI-2 and TMZ enhanced GBM cell sensitivity to TMZ. Single-cell RNA sequencing revealed high NCOA3 expression in glioma stem cells (GSCs). si-NCOA3 inhibited GSCs proliferation and self-renewal while reducing the expression of Nestin and SOX2. NCOA3 is an oncogene in GBM. In mechanism, NCOA3 promotes GBM progression by enhancing the Warburg effect. In addition, NCOA3 is also highly expressed in GSCs and significantly promotes their proliferation and self-renewal ability. NCOA3 may represent a promising therapeutic target for GBM. - Source: PubMed
Publication date: 2026/08/13
Luo QianYang JiayingYin HailinYang MeiLiang YueyangHou YixuanSun XinzeLiu JixuanZhang Ling - SUMOylation has emerged as a key regulator of chromatin and transcription, yet its contribution to lineage reprogramming remains unclear. To explore how chromatin SUMOylation influences cellular plasticity, we studied CEBPA-driven lineage reprogramming of human leukemic B-cells into macrophage-like cells. By integrating ChIP-seq, ATAC-seq, RNA-seq and chromatin-directed proteomics, we mapped the chromatin landscape and transcriptomic changes during early reprogramming. Lineage conversion triggered a dynamic rise in SUMO2/3 chromatin occupancy at CEBPA-bound sites, revealing a coordinated regulatory mechanism. Proteomic profiling of SUMO2/3- and CEBPA-associated chromatin uncovered extensive convergence and enrichment of differentiation-related transcription factors, chromatin remodelers and coregulators. Among these, NCOA3 displayed markedly increased SUMO2/3 association upon lineage conversion. NCOA3 co-occupied CEBPA- and SUMO2/3-bound chromatin regions, implying a SUMOylation-supported coregulatory role in lineage reprogramming. Pharmacological inhibition of SUMOylation using ML-792 (SUMOi) selectively enhanced CEBPA chromatin occupancy and chromatin accessibility, altered the CEBPA association of proteins, and modified NCOA3 binding dynamics. SUMOi also reshaped gene expression, promoting loss of B-cell identity and activation of macrophage-associated programs, including lipid metabolism. Collectively, our findings highlight chromatin SUMOylation as a dynamic and context-dependent modifier that fine-tunes lineage transitions, with implications for chromatin biology and therapeutic modulation of cell identity. - Source: PubMed
Publication date: 2026/05/27
Valima EmmaManjur A B M KaiserSavinainen EeviVaris VeraLaunonen Kaisa-MariGraf ThomasVarjosalo MarkkuNiskanen Einari APalvimo Jorma J - Metabolic dysfunction-associated steatotic liver disease (MASLD) and metabolic dysfunction-associated steatohepatitis (MASH) are leading causes of cirrhosis and hepatocellular carcinoma. Defects in autophagy contribute to the development of MASLD; however, the role of Unc-51-like autophagy-activating kinase 1 (ULK1) in the pathophysiology of MASLD remains unclear. Herein, we show that ULK1, a serine/threonine kinase and core autophagy protein, is significantly repressed in human MASH livers, and that hepatocyte-specific loss of ULK1 promotes, unexpectedly, hepatic steatosis and progression to liver fibrosis, without affecting basal autophagy flux. Phospho-proteomics identified the transcriptional coactivator NCOA3 as a downstream phospho-target of ULK1. Mechanistically, ULK1 phosphorylates NCOA3 to repress its transcriptional activity and restrain the CREB/CBP-mediated de novo lipogenic program. Accordingly, a phosphorylation-deficient NCOA3 mutant drives CREB/CBP-mediated lipogenesis, whereas genetic or pharmacological NCOA3 inhibition prevents steatosis, hepatic inflammation, and profibrotic signaling. Hence, ULK1-mediated NCOA3 phosphorylation is a fundamental and druggable checkpoint against the entire MASLD spectrum. - Source: PubMed
Publication date: 2026/04/02
Koo Young DoCastillo Romilia TatianaSukumaran Nair AshaGarneau MichaelGochee ChadCampbell Zachary VVakil Tashya ShreyasHa JuaMarti AlexSoto JamieDas DebajyotiMartinez-Lopez NuriaSharma ShipraDelgado YenniferPhung CallieAshley Immy AKapelczak Edmund DJacobo RashelWeatherford Eric TDai Dao-FuBenhammou Jihane NMarshall Andrea GHinton AntentorYang LingPereira Renata OTeSlaa TaraBouhaddou MehdiSingh RajatAbel E Dale - Steroid receptor co-activators (SRCs) constitute a family of transcriptional co-regulators that comprising three structurally similar members: SRC1, SRC2 and SRC3. Although extensive research has investigated the association between SRC3 and cancer, significant knowledge gaps persist. This review summarizes current research progress, identifies existing gaps, and proposes directions for future investigations. A systematic search of the PubMed database was conducted to identify literature relevant to the this topic. The study selection process, including inclusion and exclusion criteria, is presented in the accompanying figure following PRISMA guidelines. SRC3 plays a critical role in cancer development by promoting cancer cell proliferation and growth, enhancing tumor angiogenesis, modulating immune surveillance, influencing hormone signaling, and regulating diverse cytokines, including inflammatory mediators. It has been implicated in the pathogenesis of both hormonal and non-hormonal cancers. However, a substantial gap remain in clinical trials evaluating the therapeutic potential of SRC3-targeted interventions. Although research on SRC3 in hormone-related cancers is relatively comprehensive, its role in non-hormonal cancers and its clinical translation potential remain insufficiently explored. Future research should examine how SRC3 inhibition affects immune signaling pathways, the tumor and immune microenvironments, tumor heterogeneity, and various aspects of clinical translation, including novel drug development and diagnostic model design. - Source: PubMed
Publication date: 2025/12/31
Deng XiaoliangLuo YanqunGao YingWang LiqiongWu Tao - The CREB-binding protein (CBP) and its paralogue p300 are cellular integrators of various signaling pathways involved in various physiological functions. Together with NCOA proteins, they act as coactivators of nuclear receptors. CBP/p300 and NCOA3 are overexpressed in endocrine cancers, leading to enhanced nuclear receptor activity and promoting tumor progression through activation of oncogenes and regulation of cellular functions. Thus, targeting CBP/p300-NCOA3 has great potential for the development of antitumor agents. As a tool to disrupt disease-related protein-protein interactions, we developed the NCOA3 activation domain 1 (AD1) peptide containing noncanonical α-methylated amino acids for targeting the intrinsically disordered nuclear coactivator binding domain (NCBD) in CBP/p300. We showed that this peptide variant binds with a stronger affinity to its target proteins than the wild-type peptide and inhibits CBP/p300 acetylase activity. This peptide variant also modulates interactomes and CBP/p300-mediated gene transcription and exhibits effective antiproliferative activity in cell-based assays. - Source: PubMed
Publication date: 2025/12/16
Silvestri AuroraOsz JuditJouin AlexisBauer ValentinChalhoub SandraTorbeev VladimirRochel Natacha