Ask about this productRelated genes to: ZFP91 Blocking Peptide
- Gene:
- ZFP91 NIH gene
- Name:
- ZFP91 zinc finger protein
- Previous symbol:
- -
- Synonyms:
- PZF, ZNF757
- Chromosome:
- 11q12.1
- Locus Type:
- gene with protein product
- Date approved:
- 2001-03-27
- Date modifiied:
- 2016-10-05
Related products to: ZFP91 Blocking Peptide
Related articles to: ZFP91 Blocking Peptide
- Ecotropic viral integration site 1 (EVI1) is essential for hematopoietic stem cell maintenance, and its aberrant expression is a significant adverse prognostic indicator in myeloid leukemia. EVI1 overexpression typically occurs due to chromosomal rearrangement involving 3q26. However, aberrant EVI1 expression is still observed in numerous cases without 3q26 abnormalities, leading to similarly poor outcomes, while the mechanism behind EVI1 overexpression in these cases remains largely unknown. Here, we performed genome-wide CRISPR screening using cells with GFP knock-in at the EVI1 locus and identified zinc finger protein 91 (ZFP91) was the leading activator of EVI1. ZFP91 knockout significantly reduced EVI1 expression and cell proliferation. We also showed that ZFP91 binds to the EVI1 promoter, enhancing H3K4me3/H3K27ac and chromatin accessibility. Our data showed that the ZFP91-EVI1 axis plays a critical role for activation of EVI1 in myeloid leukemia. Our screening approach represents a powerful and unbiased method for identifying expression regulators that can be broadly applied across a range of contexts. - Source: PubMed
Publication date: 2026/04/25
Hayashida HirokiMasamoto YosukeOyama TakashiHino ToshiyaMorita KenFujiki KatsunoriNakato RyuichiroShirahige KatsuhikoKurokawa Mineo - BCL11A is a transcription factor crucial for neurodevelopment and hematopoiesis. It regulates the developmental switch from fetal hemoglobin (HbF) to adult hemoglobin and is a major therapeutic target for sickle cell disease and β-thalassemia. BCL11A exists in multiple isoforms, including the L isoform (containing a single two-finger ZF2-3 DNA-binding domain) and the XL isoform (containing two arrays: the two-finger ZF2-3 and the three-finger ZF4-6). We used three approaches to investigate BCL11A functions. First, we examined DNA recognition by BCL11A, which preferentially binds the short 6-bp DNA motif TGnCCA. ZF4-6 recognizes all four variants of this motif with distinct strand-specific interactions: TGtCCA on the top strand, TG(A/C)CCA on the complementary strand, and the palindromic TGgCCA on either strand. ZF2-3 also binds TGtCCA from the top strand, featuring a unique thymine interaction by ZF2 Phe388. Motif multiplicity within BCL11A binding sites may promote BCL11A oligomerization by enabling multiple ZF arrays to engage DNA simultaneously. Second, we treated HUDEP-2 cells (which express adult hemoglobin) with inhibitors targeting three epigenetic silencing marks - DNA methylation, histone H3 lysine 9 methylation or H3 lysine 27 methylation. All treatments, individually or in combination, increased HbF expression to varying degrees. Notably, FTX6058 markedly reduced BCL11A transcription and translation (likely via effects on LIN28B), while EML741 caused a partial reduction. Third, we screened 213 pomalidomide- and lenalidomide-derived compounds and quantified proportions of HbF+ cells by flow cytometry. Effects of four compounds were analyzed by protein mass spectrometry. Although BCL11A levels themselves were unchanged, all four compounds selectively decreased levels of known pomalidomide targets, with consistently decreased levels of the zinc-finger proteins IKZF1 and ZFP91. Together, our studies clarify how BCL11A recognizes DNA, how its expression can be modulated epigenetically, and how small-molecule degraders influence its regulatory network, providing new avenues for HbF reactivation therapies. - Source: PubMed
Publication date: 2026/02/08
Yu MeigenDas PuspaHorton John RZhou JujunLee JisunHong TingtingLu YueEstecio Marcos RIakova Polina AJain Abhinav KSbardella GianlucaXiong YanJin JianBlumenthal Robert MHuang YunZhang XingCheng Xiaodong - Cycle of glacial contraction and postglacial expansion in widespread European organisms, as inferred from neutral genetic markers, has led to classic phylogeographic divergence and a primarily latitudinal gradient in genetic diversity. However, the relative contribution of adaptive loci, compared to neutral loci, in shaping complex phylogeographic patterns remains poorly understood. - Source: PubMed
Publication date: 2026/01/27
Liu ChenQiao MuFu SiyingBerchi Gavril MariusDamgaard JakobMillán AndrésGuo BoxiongJin ZezhongBu WenjunYe Zhen - The substantial interest in plant-based drugs or plant-derived phytocompounds drives researchers to conduct comprehensive investigations on their therapeutic properties. Mollugin, one of the major active constituents of , has been well-studied for its pharmacological properties, demonstrating potent anti-inflammatory properties by suppressing the TAK-1-mediated activation of NF-κB/MAPK and enhancing the Nrf2/HO-1-mediated antioxidant response. It exhibits strong anticancer effects through ferroptosis via IGF2BP3/GPX4 pathways, induces mitochondrial apoptosis, and targets NF-κB, ERK, and PI3K/Akt/mTOR to suppress tumor progression. Mollugin also inhibits JAK2/STAT and PARP1 pathways, suppressing IL-1β expression via the modulation of ZFP91. Moreover, it regulates the MAPK/p38 pathway, promotes neuroprotection, and improves cognitive performance through GLP-1 receptor activation. Mollugin promotes osteogenesis by activating the BMP-2/Smad1/5/8 signaling pathway and downregulates MAPK, Akt, and GSK3β expression, leading to the inhibition of osteoclastogenesis. It overcomes multidrug resistance by downregulating MDR1/P-gp, CREB, NF-κB, and COX-2 through AMPK activation. Its antibacterial effect is mediated by strong binding to FUR, UDP, and IpxB proteins in . Mollugin mitigates infection, suppresses adipogenesis without causing cytotoxicity, and protects endothelial cells via the BDNF/TrkB-Akt signaling pathway. Synthetic derivatives of mollugin, such as oxomollugin and azamollugin, have shown enhanced anticancer and anti-inflammatory effects by regulating EGFR, PKM2, TLR4/MyD88/IRAK/TRAF6, and NF-κB/IRF3 pathways with improved solubility and stability. Collectively, these findings emphasize the broad-spectrum activity of mollugin. This review provides a critical interpretation of the mechanistic pathways regulated by mollugin and its derivatives, emphasizing their pharmacological significance and exploring their potential for future translation as multitarget drug candidates. - Source: PubMed
Publication date: 2025/12/13
Olakkengil Shajan Sandra RossZia BushraSharma CharuSubramanya Sandeep BOjha Shreesh - Colorectal cancer (CRC) is a leading cause of cancer-related mortality worldwide, with the tumor microenvironment (TME) playing a pivotal role in its progression and therapeutic resistance. The ubiquitin-proteasome system (UPS), a central regulator of intracellular protein degradation, is increasingly recognized for its involvement in cancer pathogenesis, though its specific role in modulating the CRC TME remains to be fully elucidated. This review aims to systematically summarize current evidence on how the UPS influences the immunosuppressive network within the CRC TME and to evaluate its potential as a therapeutic target. - Source: PubMed
Publication date: 2025/12/08
Wang XuanRen YiSong RuihaoLiu JiaZhou YaojunYang SihaiLiu YadongLei YiZhao Xin