Ask about this productRelated genes to: PNO1 antibody
- Gene:
- PNO1 NIH gene
- Name:
- partner of NOB1 homolog
- Previous symbol:
- KHRBP1
- Synonyms:
- RRP20
- Chromosome:
- 2p14
- Locus Type:
- gene with protein product
- Date approved:
- 2006-11-06
- Date modifiied:
- 2019-02-18
Related products to: PNO1 antibody
Related articles to: PNO1 antibody
- Trypanosomatid ribosomes display distinctive features, including extensive ribosomal RNA (rRNA) expansions and additional insertions in ribosomal proteins. Moreover, the region corresponding to the human 28S rRNA is fragmented into six molecules in these organisms with a duplication of the 3' fragment (ε) in. Although these differences suggest that ribosome biogenesis in trypanosomatids may involve unique processing events, the molecular mechanisms underlying this process are still poorly characterized. In this study, we investigated the protein composition of pre-small-subunit (pre-SSU) complexes in . We generated cell lines expressing tagged versions of UTP6 and PNO1, two conserved ribosome biogenesis factors that provide complementary access to complexes of early SSU processome intermediates and later pre-40S maturation stages. Affinity purification followed by mass spectrometry identified numerous conserved ribosome biogenesis factors alongside a substantial set of trypanosomatid-specific proteins with no assigned function. Structural analyses revealed that many of these uncharacterized proteins contain predicted RNA-binding motifs or protein-protein interaction domains, and have been previously localized to the nucleolus, supporting potential roles in ribosome synthesis. Our findings expand the repertoire of candidate SSU assembly factors in kinetoplastids and highlight species-specific adaptations in ribosome biogenesis, providing a foundation for future functional studies targeting these unique components. - Source: PubMed
Publication date: 2026/05/18
Perez Gustavo GuadagniniHiraiwa Priscila Mazzocchida Silva Verônica SantanaZanchin Nilson Ivo ToninGuimarães Beatriz Gomes - Breast cancer is a highly heterogeneous disease with diverse phenotypes. At present, increasing evidence supports the role of ribosomal biogenesis in human diseases and tumorigenesis. PNO1, as a ribosome assembly factor, plays a key role in the biological synthesis of ribosomes and ribosomal protein mutations associated with human diseases and tumor development. This study explored PNO1's role as a prognostic biomarker for breast cancer. - Source: PubMed
Wang XiaoruiYue PingLiu DongmingWen XinruiZhang XiehuaSun BoLuo YiChen LiweiLi WeidongLiu HongHe YuchaoTong ZhongshengGuo Hua - Intrahepatic cholangiocarcinoma (iCCA) represents a growing health concern due to its increasing incidence and poor prognosis, highlighting the urgent need for biomarkers and therapeutic targets. This study utilized BayesPrism deconvolution, Weighted Gene Co-expression Network Analysis (WGCNA), and Summary Mendelian Randomization (SMR), integrated with single-cell RNA sequencing (scRNA-seq) data, to analyze the tumor microenvironment. Seven distinct cell subpopulations, including Exhausted CD8 + T cells (Tex), were identified. Notably, scPagwas analysis revealed gene enrichment in UQCRH, HINT1, and AKR1C3, associated with Tex. BayesPrism analysis confirmed their increased presence in the tumor microenvironment, indicating a role in immune evasion. WGCNA identified 594 genes linked to these cells, with PNO1 and AKR1C5P emerging as potential disease-associated genes. These findings highlight the critical role of Tex in immune suppression and identify key genes for further investigation in iCCA progression and treatment strategies. - Source: PubMed
Publication date: 2025/06/13
Feng LiuXingYuan QuanYu HaoYe RongJieXie ZhenHaoXu JiaHuanLi XiuDongWang ShuangJia - The ribosome assembly factors PNO1 and NOB1 play crucial roles in the maturation of the 40S ribosomal small subunit. TurboID is an efficient biotin ligase that can biotinylate proteins in proximity to the target protein and is widely used to study complex biological processes within cells. In this study, we employed this technology to investigate the complex proximity network of PNO1 and NOB1 within the cell, further revealing their key roles in ribosome biogenesis. - Source: PubMed
Publication date: 2025/03/27
Xu XingyuanChen WenliZheng JiefuLiao Jian-YouYan HaiyanZhu Shuang - PNO1, a key promoter of oncogenesis, is often characterized by its aberrant expression in both colorectal and esophageal cancers, markedly accelerating their progression. Nonetheless, the role of PNO1 in ovarian cancer and its underlying mechanisms remain unexplored comprehensively. In addition to the abnormal PNO1 expression in ovarian cancer tissues by The Cancer Genome Atlas (TCGA) database, the clinical data examinations indicated its strong association with lower survival rates among ovarian cancer patients. Considering the crucial role of the AKT signaling pathway, we hypothesized that PNO1 might drive the progression of ovarian cancer by modulating the AKT pathway. To validate this hypothesis, experiments were conducted to silence PNO1 in ovarian cancer cells. These findings demonstrated that PNO1 silencing markedly reduced the proliferation and invasion capabilities of ovarian cancer cell lines, triggering their apoptosis. Moreover, the PNO1 suppression significantly decreased the expression levels of p-AKT, GSK-3β, and active β-catenin proteins, further confirming the regulatory correlation between PNO1 and the AKT/Wnt/β-catenin pathway. The oncogenic effects mediated by the PNO1-activated Wnt/β-catenin pathway were counteracted by inhibitors of the AKT signaling pathway. Further, the subcutaneous xenograft tumor assays in vivo validated that PNO1 silencing decreased the tumorigenic potential of ovarian cancer cells. In summary, this study has elucidated that the upregulation of PNO1 modulated the tumorigenic role of the AKT/Wnt/β-catenin pathway in ovarian cancer, offering new insights into its oncogenic function. - Source: PubMed
Publication date: 2025/03/20
Qin LuLu JiaoQian QiaohongTang MinjieLiu Min