| 2003 |
Yeast RRP20 (ortholog of human PNO1) is a nucleolar protein required for pre-18S rRNA processing; a Gly235Asp mutation in its KH-type RNA-binding domain causes marked deficiency in 18S rRNA production by impairing early pre-rRNA cleavages at sites A1 and A2, leading to accumulation of a 22S dead-end processing product. RRP20 is present in 90S pre-ribosomal particles. |
Northern blotting, primer extension analysis, point mutagenesis, in S. cerevisiae |
Nucleic acids research |
High |
12736301
|
| 2004 |
Human PNO1 protein (~35 kDa) localizes to the nucleus and specifically to nucleoli; deletion analysis showed that residues 92–230 are solely responsible for nucleolar retention, and the KH domain alone is insufficient for this localization. |
GFP fusion expression and subcellular localization of 13 deletion constructs in mammalian cells, Western blot |
DNA sequence : the journal of DNA sequencing and mapping |
Medium |
15497447
|
| 2012 |
Homozygous Pno1 knockout in mice causes early embryonic lethality with arrest before the compaction stage, demonstrating that Pno1 is essential for early development. Density gradient fractionation showed that overexpressed tagged Pno1 exists in large complexes with sedimentation rates between 20S and 26S, distinct from mature 26S proteasomes, 40S, and 60S ribosomal subunits. |
Gene knockout mouse generation, ex vivo embryo development assay, density gradient fractionation |
PloS one |
Medium |
23029399
|
| 2019 |
PNO1 knockdown in colorectal cancer cells (HCT116) decreased levels of 18S rRNA, 40S and 60S ribosomal subunits, and 80S ribosomes, and reduced global protein synthesis; this increased nucleolar stress and inhibited MDM2-mediated ubiquitination and p53 degradation, resulting in p53 and p21 upregulation. EBF1 suppresses PNO1 promoter activity and reduces PNO1 mRNA and protein levels. |
shRNA knockdown, ribosome fractionation, Western blot, luciferase promoter assay, p53 knockout rescue, p53 inhibitor PFT-α rescue, in vitro and xenograft in vivo experiments |
Cancer research |
High |
30862720
|
| 2019 |
PNO1 knockdown in hepatocellular carcinoma cells suppressed tumor growth and metastasis and significantly reduced AKT/mTOR signaling, implicating PNO1 in activation of this pathway. |
Lentiviral shRNA knockdown, Western blot, in vitro and xenograft in vivo experiments |
Medical science monitor |
Low |
31568401
|
| 2020 |
EBF1 overexpression in colorectal cancer cells downregulates PNO1 mRNA and protein expression and transcriptional activity, while upregulating p53 and p21 proteins, suppressing cell growth and inducing apoptosis. |
Lentiviral transduction of EBF1, luciferase promoter assay for PNO1 transcriptional activity, Western blot, in vitro and in vivo assays |
Frontiers in oncology |
Medium |
32676457
|
| 2020 |
miR-340-5p directly binds the 3′ UTR of PNO1 mRNA and represses its expression; PNO1 knockdown inhibits the Notch signaling pathway, which in turn modulates epithelial–mesenchymal transition (EMT) in lung adenocarcinoma cells. |
Luciferase 3′ UTR reporter assay, miRNA overexpression/knockdown rescue experiments, in vitro invasion and proliferation assays, in vivo xenograft |
Oncogenesis |
Medium |
32483111
|
| 2021 |
PNO1 physically interacts with THBS1, and simultaneous silencing of THBS1 attenuates or reverses the pro-tumorigenic effects of PNO1 overexpression in glioma cells; PNO1 activates FAK/Akt signaling downstream of this interaction. MYC overexpression increases PNO1 promoter activity, placing MYC upstream of PNO1. |
Co-immunoprecipitation (PNO1–THBS1 interaction), THBS1 siRNA rescue, luciferase promoter assay for MYC→PNO1, Western blot for FAK/Akt, in vitro and in vivo assays |
Cell death & disease |
Medium |
33664245
|
| 2021 |
PNO1 promotes hepatocellular carcinoma progression through the MAPK signaling pathway, as demonstrated by RNA-seq analysis combined with functional experiments following PNO1 overexpression and knockdown, and associated modulation of autophagy and apoptosis. |
RNA-seq, Western blot for MAPK pathway components, overexpression/knockdown in vitro and in vivo |
Cell death & disease |
Low |
34050137
|
| 2021 |
PNO1 knockdown in esophageal cancer cells downregulates CTNNB1 (β-catenin) among other proteins, and overexpression of CTNNB1 reverses the anti-proliferative and pro-apoptotic effects of PNO1 knockdown, placing CTNNB1 downstream of PNO1. |
shRNA knockdown, CTNNB1 overexpression rescue, Western blot, in vitro proliferation and apoptosis assays |
Oncology reports |
Low |
33864661
|
| 2022 |
PNO1 knockdown in triple-negative breast cancer cells arrests cell cycle at G2/M phase and downregulates cyclin B1 (CCNB1) and CDK1 protein expression; PNO1 expression is positively correlated with CDK1 and CCNB1 in patient samples. |
Lentiviral shRNA knockdown, flow cytometry cell-cycle analysis, Western blot, in vitro and xenograft in vivo experiments |
Oncology reports |
Low |
35445733
|
| 2022 |
The transcription factor E2F6 binds the PNO1 promoter and upregulates PNO1 expression; this is part of a circ_0004676/miR-377-3p/E2F6/PNO1 regulatory axis in triple-negative breast cancer. |
RIP assay, RNA pull-down, FISH, RT-qPCR, Western blot for promoter binding of E2F6 to PNO1 |
Cell biology and toxicology |
Medium |
35870038
|
| 2024 |
PNO1 knockdown suppresses CRC cell growth, proteasome activities and assembly, and inhibits CDKN1B/p27Kip1 (p27) degradation via the proteasome; p27 knockdown partially rescues the growth inhibition caused by PNO1 knockdown, placing PNO1 upstream of proteasome assembly and p27 stability. miR-326 directly targets the CDS region of PNO1 mRNA to suppress its protein expression and thereby reduce proteasome activity. |
shRNA knockdown, miR-326 overexpression, proteasome activity assay, Western blot for p27, luciferase/reporter assay for miR-326 binding, rescue by p27 knockdown |
Scientific reports |
Medium |
39414903
|
| 2024 |
PNO1 is described as collaborating with NOB1 in the maturation of 20S pre-rRNA into functional 18S rRNA and in maturation of the 40S ribosomal small subunit; PNO1 and NOB1 are positioned within the pre-40S subunit. |
Review/summary of existing literature (no new direct experiment reported in this abstract) |
Current pharmaceutical design |
Low |
39143880
|
| 2025 |
PNO1 and NOB1 have distinct subcellular localizations as shown by immunofluorescence; proximity labeling (TurboID) identified 871 proximal proteins for PNO1, with 663 overlapping with NOB1 proximal proteins. Co-IP experiments confirmed that PNO1 interacts with translation-related proteins EIF4B and EIF4G2. |
TurboID proximity labeling, mass spectrometry, co-immunoprecipitation (Co-IP), immunofluorescence |
Gene |
Medium |
40157618
|
| 2025 |
PNO1 silencing in ovarian cancer cells decreases p-AKT, GSK-3β, and active β-catenin protein levels, and AKT signaling pathway inhibitors counteract the oncogenic effects of PNO1-activated Wnt/β-catenin signaling, placing PNO1 upstream of the AKT/Wnt/β-catenin pathway. |
siRNA knockdown, Western blot for AKT/Wnt pathway components, AKT inhibitor pharmacological rescue, xenograft in vivo assay |
Scientific reports |
Low |
40113869
|
| 2025 |
PNO1 promotes breast cancer stem-like properties through activation of the NF-κB signaling pathway; JSH-23 (NF-κB inhibitor) suppresses these PNO1-dependent stemness effects. |
shRNA knockdown, RNA-seq, sphere-formation assay, Western blot, flow cytometry, pharmacological inhibition (JSH-23), in vitro and in vivo |
Stem cells (Dayton, Ohio) |
Low |
40971713
|