ArticleJournal of translational medicine2026
DUSP4-mediated dephosphorylation of PSMD14 enhances PSMD14-dependent deubiquitination of MICALL2 and promotes malignant progression in clear cell renal cell carcinoma.
Article in Journal of translational medicine, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
1 citing paper in PubMed.
- PSMD14 as a translational target in cancer and beyond: from deubiquitination mechanisms to drug resistance and precision therapy.Cancer drug resistance (Alhambra, Calif.) · 2026Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundPSMD14 has been identified as an oncogene in various cancers; however, its role in clear cell renal cell carcinoma (ccRCC) remains unclear. This study investigated the effects of PSMD14 on ccRCC cell proliferation, migration, and invasion.
methodsThirty paired cancerous and adjacent non-cancerous tissues were collected from patients with ccRCC. The human normal renal tubular epithelial cell line HK-2 and ccRCC cell lines (KMRC-1, OS-RC-2, Caki-1, and 786-O) were used for in vitro experiments. The mRNA and protein expression levels of PSMD14, MICALL2, and DUSP4 were analyzed by RT-qPCR and Western blotting. Cell viability and proliferation were evaluated using the CCK-8 assay and EdU staining. Wound-healing and Transwell assays were performed to assess cell migration and invasion, respectively. Co-immunoprecipitation was conducted to verify molecular interactions between PSMD14 and MICALL2/DUSP4. Immunoprecipitation was used to examine MICALL2 ubiquitination and PSMD14 phosphorylation. An in vivo ccRCC mouse model was established to assess tumor growth. Immunohistochemical staining was used to detect Ki67 and PSMD14 expression in mouse tumor tissues.
resultsPSMD14 was significantly upregulated in ccRCC tissues and was correlated with poor patient outcomes. PSMD14 knockdown inhibited ccRCC cell proliferation, migration, and invasion. PSMD14 suppressed MICALL2 ubiquitination and degradation, thereby increasing MICALL2 expression and promoting ccRCC malignant progression. Dephosphorylation of PSMD14 by DUSP4 enhanced its interaction with MICALL2. Moreover, DUSP4-mediated dephosphorylation amplified the PSMD14-induced increase in MICALL2, further facilitating ccRCC progression. In vivo, PSMD14 knockdown inhibited ccRCC tumor development.
conclusionDUSP4-mediated dephosphorylation of PSMD14 promotes ccRCC malignant progression by regulating MICALL2 deubiquitination, providing potential therapeutic targets for ccRCC treatment.
Indexed as
Identifiers
What Socratic holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.