Ask about this productRelated 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
- 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 - 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 - Myocardial fibrosis (MF) represents a major pathological alteration observed in the progression of numerous heart conditions. The presence of excessive MF is key in the progression of numerous heart diseases, which may lead to heart failure. Abnormal expression of pumilio RNA-binding family member 2 (PUM2), an RNA-binding protein, is a contributing factor in the development of a variety of diseases. The present study aimed to investigate how PUM2 affected the expression and alternative splicing of genes associated with MF in H9C2 cells, thus evaluating the role of PUM2 in this context. Inhibition of PUM2 expression in H9C2 cardiomyocytes was achieved through small interfering RNA transfection. Cell viability was assessed using a Cell Counting Kit-8 assay, while apoptosis was detected through flow cytometry. RNA-sequencing (RNA-seq) was utilized to analyze the differential gene expression profiles and alternative splicing events (ASEs) in H9C2 cells regulated by PUM2. Sequencing results were confirmed through reverse transcription-quantitative PCR. The results showed that a reduction in PUM2 levels inhibited cell viability without affecting apoptosis. RNA-seq analysis revealed notable changes in the expression of various genes associated with MF, including adrenomedullin, NDRG family member 4, phospholipid phosphatase 3, integrin subunit α 8, regulator of G protein signaling 2, cadherin 11, integrin subunit α 11 and transforming growth factor β-induced, following PUM2 knockdown. In addition, PUM2 regulated ASEs in genes associated with fibrosis progression, such as tropomyosin 1 and actinin α1. The present study revealed that PUM2 had a regulatory effect on alternative splicing and gene expression associated with MF, suggesting PUM2 as a promising molecular target for MF therapy. - Source: PubMed
Publication date: 2026/02/04
Zhang ZilongZhou HangyuAdili DiliyaerZhu WeiLiu YongZhou WenzhengWang ZhaoLi Jie - Pumilio proteins are conserved RNA-binding proteins that control mRNAs involved in development, proliferation, and differentiation. Human PUM1 and PUM2 repress targets by recruiting the CCR4-NOT deadenylase complex through a metazoan-specific, intrinsically disordered repression domain (RD3). Here we dissect RD3 using functional assays, protein interaction assays, and crosslinking mass spectrometry. We identify multiple RD3 peptides that are sufficient for repression and binding to the CCR4-NOT complex. Crosslinking reveals numerous mutually exclusive contacts between RD3 and CCR4-NOT, consistent with a multivalent "fuzzy" binding mode in which interactions are not defined by a single sequence or structure. Sequence scrambling shows that the linear amino acid order of RD3 is dispensable, whereas its physicochemical composition, in particular aliphatic and aromatic residues, is essential for repression and CCR4-NOT binding. These findings support a model in which multivalent interactions between intrinsically disordered regions and effector complexes, governed by amino acid composition, underlie robust PUM-mediated repression and exemplify general principles by which intrinsically disordered regions recruit CCR4-NOT to regulate gene expression. - Source: PubMed
Publication date: 2026/02/12
Dunshee Elise BSaladin Brenna ATurner David JQiu ChenDutcher Robert CWilliams Jason GCorbo JoshuaWolcott Olivia RKorte Amanda JHaugen Rebecca JTanaka Hall Traci MValkov EugeneGoldstrohm Aaron C