| 2003 |
Rpn5 (PSMD12 ortholog in fission yeast) is a lid subunit of the 26S proteasome that associates with the proteasome and is required for proper proteasome assembly and localization around the inner nuclear membrane. Deletion of rpn5 leads to accumulation of polyubiquitinated proteins (e.g., Cut2/securin) and mitotic abnormalities. Nuclear import of Rpn5 requires other lid components, while subsequent assembly into the nuclear membrane requires the base subcomplex. Human Rpn5 rescues rpn5Δ phenotypes and is incorporated into the yeast proteasome, demonstrating functional conservation. |
Genetic deletion (rpn5Δ), overexpression, fluorescence localization, epistasis with lid/base mutants, complementation with human PSMD12 |
The Journal of biological chemistry |
High |
12783882
|
| 2018 |
The N-terminal domain (NTD) of yeast Rpn5 (PSMD12 ortholog) adopts an α-solenoid-like fold in a right-handed superhelical configuration formed by multiple α-helices, as determined by NMR spectroscopy. The NTD is conformationally flexible and contains three putative protein-interaction sites. Structural comparisons reveal local differences in the first three helices between yeast and human Rpn5. |
NMR spectroscopy (solution structure determination of Rpn5 NTD residues 1–136); structural comparison with cryo-EM data |
Biochemical and biophysical research communications |
Medium |
30177392
|
| 2018 |
The Rpn5 (PSMD12) subunit, located in the lid subcomplex of the 19S regulatory particle, inhibits Rpn11 deubiquitinase activity in the isolated lid. The NTD (α-solenoid domain) is highly flexible in the isolated lid and may participate in interactions with different proteasome subunits. |
NMR resonance assignment (1H, 13C, 15N backbone and side chain) of Rpn5 NTD; referenced established biochemical knowledge about Rpn11 inhibition |
Biomolecular NMR assignments |
Low |
30229448
|
| 2022 |
PSMD12 interacts with influenza A virus M1 protein and promotes K63-linked ubiquitination of M1 at the K102 site, thereby facilitating M1-M2 virus-like particle release and viral budding. PSMD12 knockdown or M1-K102 mutation disrupts virus budding and reduces viral replication and virulence in mice. |
Immunoprecipitation/mass spectrometry (identification of interaction), Co-IP, site-directed mutagenesis of M1-K102, VLP release assay, transmission electron microscopy, reverse-genetics mutant viruses, mouse virulence experiments |
Journal of virology |
High |
35861516
|
| 2022 |
PSMD12 haploinsufficiency impairs proteasome function in peripheral blood mononuclear cells and in PSMD12-knockdown HEK 293T cells, leading to elevated type I interferon signaling especially in monocytes, as part of a proteasome-associated autoinflammatory syndrome (PRAAS) phenotype. |
Whole-exome sequencing (variant identification), proteasome activity assays in patient PBMCs and PSMD12-knockdown HEK 293T cells, single-cell RNA sequencing |
Arthritis & rheumatology (Hoboken, N.J.) |
Medium |
35080150
|
| 2023 |
PSMD12 physically interacts with CDKN3 (cyclin-dependent kinase inhibitor 3) and reduces its ubiquitination level, thereby stabilizing CDKN3 protein and promoting pancreatic cancer cell proliferation. Rescue assays confirmed that CDKN3 regulation mediates the proliferative and anti-apoptotic effects of PSMD12. |
Co-immunoprecipitation, Western blot (ubiquitination assay), rescue/epistasis assays, xenograft models |
Cancer gene therapy |
Medium |
37037907
|
| 2025 |
PSMD12 interacts with CDK1, prevents its proteasome-mediated degradation through deubiquitination (reducing CDK1 ubiquitination), thereby stabilizing CDK1 and accelerating G2/M cell cycle progression in hepatocellular carcinoma cells. |
Co-immunoprecipitation, Western blot, cycloheximide chase, MG132 proteasome inhibition assay, CRISPR-Cas9 knockout, lentiviral overexpression, xenograft experiments |
Frontiers in immunology / Cancer science (replicated in two independent papers) |
High |
40534847 41496578
|
| 2021 |
PSMD12 increases the protein level of Nrf2 transcription factor and promotes Nrf2 nuclear translocation, which then drives glioma cell proliferation and invasion via Akt signaling-mediated Nrf2 expression. Nrf2 overexpression rescues the inhibitory effects of PSMD12 knockdown. |
siRNA knockdown, overexpression, Western blot, CCK-8, Transwell invasion assay, xenograft model, epistasis rescue experiments |
Annals of translational medicine |
Medium |
33987398
|
| 2024 |
PSMD12 elevates Nrf2 protein level and promotes its nuclear translocation, which increases TrxR1 promoter activity and TrxR1 transcription, promoting NSCLC progression. TrxR1 overexpression rescues the suppressive effects of PSMD12 knockdown. |
siRNA knockdown, overexpression, Western blot, dual luciferase reporter assay (Nrf2 on TrxR1 promoter), immunofluorescence staining, flow cytometry, Transwell assay, rescue experiments |
Genes & genomics |
Medium |
38243044
|
| 2024 |
RPS27A (ubiquitin-ribosomal protein S27a) regulates PSMD12 expression, and silencing RPS27A in OGD/R-induced microglia and MCAO mice attenuates inflammatory factor release and neutrophil infiltration via modulation of the PSMD12/NF-κB signaling axis. |
siRNA silencing of RPS27A in OGD/R microglia and MCAO mouse model, high-throughput sequencing, GO/KEGG/PPI analysis, immunological assays for inflammatory factors and immune cell infiltration |
Molecular medicine (Cambridge, Mass.) |
Low |
39039432
|
| 2020 |
PSMD12 knockdown in breast cancer cells activates the apoptosis pathway by upregulating pro-apoptotic genes TXNIP, GADD45A, GADD45B, RHOB, and CDKN1A, as identified by RNA-seq and validated by RT-qPCR and Western blot. Restoration of PSMD12 expression decreases expression of these pro-apoptotic genes. |
siRNA knockdown, RNA-seq, RT-qPCR, Western blot, flow cytometry, GeCKO screen, mouse xenograft |
Biochemical and biophysical research communications |
Medium |
32222279
|