ZMYND8 Antibody (OAAF02745)
- Known as:
- ZMYND8 Antibody (OAAF02745)
- Catalog number:
- oaaf02745
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- ZMYND8 Antibody (OAAF02745)
Related genes to: ZMYND8 Antibody (OAAF02745)
- Gene:
- ZMYND8 NIH gene
- Name:
- zinc finger MYND-type containing 8
- Previous symbol:
- PRKCBP1
- Synonyms:
- RACK7
- Chromosome:
- 20q13.12
- Locus Type:
- gene with protein product
- Date approved:
- 1999-10-19
- Date modifiied:
- 2016-02-15
Related products to: ZMYND8 Antibody (OAAF02745)
Related articles to: ZMYND8 Antibody (OAAF02745)
- The zinc finger MYND-type containing eight protein (ZMYND8) is a chromatin reader that regulates neuronal gene expression by controlling the microtubule-associated protein tau (MAPT) locus. Here, we investigate how ZMYND8 regulates expression of the long non-coding RNA MAPT213 through its interaction with GATA zinc finger domain containing 2A (GATAD2A), a component of the Nucleosome Remodelling and Deacetylase complex. ZMYND8 exhibits opposite regulatory effects on protein-coding MAPT and non-coding MAPT213 transcripts in a manner dependent on its MYND domain, promoting MAPT expression while suppressing MAPT213 levels. Chromatin immunoprecipitation experiments demonstrated that ZMYND8 specifically recruits GATAD2A to the MAPT213 internal regulatory region, establishing a direct link between protein binding and transcriptional control. We determined the crystal structure of the ZMYND8 coiled-coil MYND domain at high resolution, revealing a homodimeric architecture. The MYND domain specifically recognizes GATAD2A through direct interaction with proline-rich motifs in GATAD2A's central region. Structure-function analysis identified critical binding interface residues, while quantitative measurements revealed moderate-affinity interactions enhanced through multivalent binding mechanisms. These findings establish the molecular basis for ZMYND8-mediated recruitment of chromatin remodeling complexes to specific genomic loci and provide a structural framework for understanding transcriptional regulation of MAPT213. - Source: PubMed
Publication date: 2026/04/16
Srivastava Dushyant KumarNandi SandhikKarmakar AvradeepDas ChandrimaRoy Siddhartha - Not available. - Source: PubMed
Publication date: 2026/04/16
Cruz-Rodriguez Nataly - Carfilzomib (CFZ) is a cornerstone therapy for patients with relapsed multiple myeloma (MM); however, poor prolonged treatment response remains a major clinical limitation. ZMYND8 overexpression increases the sensitivity of MM cells to CFZ. Therefore, pharmacological activation of ZMYND8 may offer an emerging strategy to improve CFZ efficacy. In this study, we identified a novel retinoic acid analog, WYC-209, as an epigenetic activator of ZMYND8 expression in MM cells. The additive cytotoxic effects of WYC-209 and CFZ were analyzed using flow cytometry, transmission electron microscopy, and drug synergy assays. The in vivo therapeutic synergy was assessed in a mouse xenograft model using tumor burden and survival analysis. We found that both all-trans retinoic acid (ATRA) and WYC-209 significantly upregulated the transcriptional expression of ZMYND8 by remodeling the epigenetic landscape, particularly via H3K27ac. Combined treatment with CFZ and either ATRA or WYC-209 exhibited pronounced synergistic effects in killing primary MM cells. Moreover, WYC-209 synergized with CFZ to inhibit cell viability, induce apoptosis, and exacerbate endoplasmic reticulum dilation in MM cells, whereas the depletion of ZMYND8 markedly attenuated these effects. In vivo experiments confirmed that WYC-209 potentiated the antitumor efficacy of CFZ by upregulating ZMYND8, thereby ameliorating tumor burden in NSG mice. These findings establish that targeting ZMYND8 with the novel retinoid WYC-209 potently enhances the efficacy of CFZ and holds translational promise for improving clinical outcomes in patients with MM. - Source: PubMed
Publication date: 2026/03/30
Xu JiaxuanYan JieZhang HaoyuDong JiahuiWu YueQian JiajiaZhao QuanDong XiaoqingChen Bing - - Source: PubMed
Publication date: 2026/03/27
- The cardiac complications caused by drugs, including cardiac dysfunction and heart failure, significantly limit the wide clinical application of drugs and lead to morbidity and mortality. High mobility group box 1 (HMGB1) plays an extensive role in drug-induced cardiotoxicity. However, the cardiotoxic mechanisms for most small-molecule kinase inhibitors (SMKIs) remains unknown. Here, we identify that accumulated HMGB1 is associated with the cardiac complications caused by a series of FDA-approved SMKIs, among which trametinib-induced cardiomyocyte death was most significantly reversed by HMGB1 knockout. Moreover, cardiomyocyte-specific Hmgb1 deletion in mice could improve cardiac muscle contraction, calcium regulation and cardiomyocyte apoptosis in autophagy- or inflammation-independent manner. We further show that trametinib leads to the aberrant accumulation of HMGB1 by increasing its stability via inhibiting zinc finger protein Zinc Finger MYND-Type Containing 8 (ZMYND8)-mediated ubiquitination and proteasomal degradation of HMGB1, identifying ZMYND8 as a novel negative regulator of HMGB1 stability in cardiomyocyte and a potential novel regulator of cardiac function. Glycyrrhizic acid, an HMGB1 inhibitor used in clinic, prevents trametinib-induced cardiac complications. These findings reveal the mechanism and propose an effective intervention strategy for trametinib-induced cardiac complications, which would contribute to the safe application of trametinib, cardiac safety evaluation of drugs or candidate compounds and novel drug development. - Source: PubMed
Publication date: 2025/12/19
Fu HuangxiJiang FengXu AnqiZhou TaichengLiu NingChen XueqinGao ZizhengWu WentongYan HaoYang XiaochunYang BoHe QiaojunLuo PeihuaXu Zhifei