PUM2 antibody
- Known as:
- PUM2 (anti-)
- Catalog number:
- orb137522
- Product Quantity:
- 50 ug
- Category:
- -
- Supplier:
- Biorb
- Gene target:
- PUM2 antibody
Related genes to: PUM2 antibody
- Gene:
- PUM2 NIH gene
- Name:
- pumilio RNA binding family member 2
- Previous symbol:
- -
- Synonyms:
- PUMH2, KIAA0235
- Chromosome:
- 2p24.1
- Locus Type:
- gene with protein product
- Date approved:
- 2001-03-27
- Date modifiied:
- 2015-11-05
Related products to: PUM2 antibody
Related articles to: PUM2 antibody
- Prostate cancer (PC) is one of the most common malignancies in men, and the emergence of androgen receptor-low/negative castration-resistant PC (ARL/- CRPC) following androgen receptor signaling inhibitor (ARSI) therapy remains a critical clinical challenge. The RNA-binding protein DEAD-box helicase 3 X-linked (DDX3X) has been implicated in the translational regulation of androgen receptor (AR) mRNA; however, the underlying binding mechanisms are not well defined. Here, we show that DDX3X colocalizes with AR mRNA in ARL/- CRPC cells and selectively recognizes non-canonical RNA G-quadruplex (rG4) motifs within the sequence of AR mRNA. RNA immunoprecipitation sequencing (RIP-seq) revealed enrichment of DDX3X-AR mRNA interactions in ARL/- CRPC cells. Fluorescence imaging confirmed the colocalization of DDX3X and AR mRNA within cytoplasmic granules, and biochemical assays confirmed the ability of selected AR mRNA fragments to form rG4 structures bound by DDX3X. Proteomic profiling of DDX3X-Ras GTPase-activating protein-binding protein 1 (G3BP1) complexes identified several RNA-binding proteins, including IGF2BP1, PUM2, and UBAP2, which may act as candidate cofactors. Together, these findings shed light on the interaction between AR mRNA and DDX3X and identify putative protein partners, offering insights into future therapeutic strategies. - Source: PubMed
Publication date: 2026/05/04
Zhang HanLiu Teresa TWu FeixuanColah Avan NRicke Emily ALi LingjunPutnam Andrea ARicke William A - Sporadic inclusion body myopathy (sIBM) is the most common progressive degenerative skeletal muscle disease of older people with poorly understood pathogenesis. We assessed the involvement and impact of the noncoding RNA activated by DNA damage (NORAD) and its binding partner Pumilio (PUM) proteins on the evolution of the disease process in muscle biopsies from sIBM patients with mild or severe histopathologic changes. A disease severity-dependent increase in NORAD and PUM2 expression was present along with subsarcolemmal formations of NORAD-PUM (NP) bodies in the sIBM muscles. Similarly, Norad, Pum1, and Pum2 expression levels were upregulated as disease severity increased with age in VCP-A232E mice, a model for hereditary IBM. Crossbreeding VCP-A232E mice with Norad-/- mice leading to generation of VCP mutants with either single copy or the absence of Norad showed that Norad suppresses disease progression in the VCP-A232E model in a dose-dependent manner. Norad expression in the muscle from Pum2 overexpressing mice revealed significantly increased Norad transcripts in response to high Pum2 expression and the presence of NP bodies coalescing around muscle nuclei. Collectively, these findings provide strong evidence that elevated NORAD expression is a protective, compensatory response to disease-related induction of PUM2 activity in muscle. - Source: PubMed
Publication date: 2026/04/17
Tong LingyingOzes BurcakMoss KyleMyers MorganHornung AlexandraShowalter EmmaChornyy SergiyMendell Joshua TSahenk Zarife - Pulmonary hypertension (PH) is a lethal vascular disorder characterized by obstructive remodelling of pulmonary arteries, driven predominantly by pathological phenotypes of pulmonary artery smooth muscle cells (PASMCs), including excessive proliferation, migration, and resistance to apoptosis. While the RNA-binding protein PUM2 and the potassium channel KCNK3 have been implicated in cardiovascular pathophysiology, their functional interplay in hypoxic pulmonary vascular remodelling remains undefined. Here, using rat models of PH (Sugen5416/hypoxia and monocrotaline), human PASMCs, and mechanistic assays, we identify a signalling axis in which hypoxia induces HIF1α-dependent transcriptional upregulation of PUM2. PUM2 in turn binds the 3'UTR of KCNK3 mRNA, destabilizing the transcript and reducing KCNK3 protein expression. Knockdown of PUM2 restored KCNK3 expression, promoted apoptosis, and suppressed proliferation and migration in PASMCs, whereas PUM2 overexpression exerted opposing effects. These phenotypic changes were reversed by concomitant KCNK3 knockdown, confirming KCNK3 as a critical downstream effector. In vivo, AAV9-mediated PUM2 knockdown ameliorated haemodynamic impairment, vascular remodelling, and right ventricular hypertrophy in PH rats, whereas PUM2 overexpression exacerbated disease progression. Notably, the related family member PUM1 exhibited similar hypoxia-induced upregulation and direct binding to KCNK3 mRNA, suggesting potential functional redundancy within the Pumilio family. Collectively, our results unveil a Pumilio-dependent post-transcriptional mechanism as a central driver of PASMC dysfunction in PH and nominate PUM2-and potentially other Pumilio family members-as promising therapeutic targets for mitigating hypoxic pulmonary vascular remodelling. - Source: PubMed
Publication date: 2026/04/06
Deng XiaodongZhu FaqiGuo YingZhang QiLuo XuLv ShengXu JingLiu Yi - N6-methyladenosine ([Formula: see text]) plays a crucial role in enriching RNA functional and genetic information. While deep learning has advanced [Formula: see text] site identification, current state-of-the-art methods, particularly those based on large-scale Pre-trained Language Models (PLMs), often suffer from high computational complexity and over-parameterization, limiting their scalability for genome-wide analysis. - Source: PubMed
Publication date: 2026/03/19
Gao XiaoJia JianhuaHui CongLin Yang - Ulcerative colitis (UC) is a chronic, relapsing inflammatory disorder characterized by persistent mucosal immune activation and compromised epithelial barrier function. In this study, we identify the RNA-binding protein PUMILIO2 (Pum2) as a previously unrecognized regulator of intestinal inflammation. Analysis of colonic tissues from UC patients revealed reduced Pum2 expression, which inversely correlated with disease activity. In dextran sulfate sodium (DSS)-induced colitis models, Pum2 deficiency exacerbated mucosal injury, accompanied by heightened macrophage inflammation. Mechanistically, Pum2 loss during colitis drives macrophage hyperactivation and TNFα-dependent epithelial necroptosis, which together intensify pathogenic macrophage-epithelial interactions and barrier breakdown. The dynamic downregulation of Pum2 in active inflammation underscores its potential as a therapeutic target for modulating macrophage-epithelial interactions and restoring intestinal barrier integrity in the context of colitis. Abstract Figure. Pum2 deficiency aggravates colitis via macrophage-epithelial crosstalk driving inflammation and necroptosis. Left: Pum2 loss promotes macrophage-driven inflammation, with increased chemokine expression, macrophage infiltration, and a pro-inflammatory phenotype characterized by TNFα secretion. Right: Macrophage-epithelial crosstalk triggers epithelial necroptosis. Proinflammatory signals from Pum2-deficient macrophages sensitize epithelial cells to TNFα-induced death. Simultaneously, epithelial Pum2 loss elevates ROS, facilitating RIPK1, RIPK3, and MLKL phosphorylation. This synergistic cascade amplifies necroptosis and establishes a self-perpetuating loop of barrier disruption and inflammation. - Source: PubMed
Publication date: 2026/03/20
Wang XuefeiHan XiaoxiaoQiu WenlinJiang LijuanDuan XiaoruLiu Xiaojing