Ask about this productRelated genes to: PSMD11 antibody
- Gene:
- PSMD11 NIH gene
- Name:
- proteasome 26S subunit, non-ATPase 11
- Previous symbol:
- -
- Synonyms:
- S9, p44.5, MGC3844, Rpn6
- Chromosome:
- 17q11.2
- Locus Type:
- gene with protein product
- Date approved:
- 1997-02-19
- Date modifiied:
- 2016-10-05
Related products to: PSMD11 antibody
Related articles to: PSMD11 antibody
- Hepatocellular carcinoma (HCC) is a highly aggressive malignancy characterized by unfavorable clinical outcomes. Identifying novel biomarkers and therapeutic targets is essential for advancing HCC management. Although DBF4 zinc finger B (DBF4B) has been associated with the progression of various cancers, its specific role in HCC remains poorly understood. - Source: PubMed
Publication date: 2026/08/13
Dong BingXi PengjuYang GuangxinJiao ZhiqiXu ShijieHan LinGao Zhenming - Heart failure (HF) resulting from chronic systolic overload is associated with increased burden on proteostasis and impaired proteasome function. Phosphorylation of proteasome subunit RPN6/PSMD11 at Ser14 (pS14-RPN6) mediates the activation of 26S proteasomes by PKA, but its significance in common forms of heart disease remains obscure. Hence, we investigated the impact of genetic blockade of pS14-RPN6 on cardiac remodeling and HF during systolic overload, a common condition occurring in hypertension and aortic stenosis. We detected marked increases in ubiquitin conjugates, along with elevated levels of RPN6 and pS14-RPN6 proteins in myocardial tissues from human patients with nonischemic HF. Similarly, myocardial pS14-Rpn6 was increased in wild-type mice 2 and 4 weeks after transverse aortic constriction (TAC). Compared with wild-type littermates, mice with genetic blockade of pS14-Rpn6 resulting from germline knock-in of Rpn6 (S14A mice) developed greater cardiac hypertrophy, fibrosis, left ventricular dysfunction, and lung congestion after TAC. Mechanistically, TAC induced comparable increases in 26S and 30S proteasomes at 2-week in both genotypes but, at 4-week post-TAC, the increases were remarkably attenuated in S14A mice. Meanwhile, TAC-induced increases in proteasome peptidase activities were significantly attenuated (2-week) or abolished (4-week) in S14A mice, accompanied by greater increases in total and K48-linked ubiquitin conjugates. Collectively, these findings demonstrate that pS14-RPN6 plays an essential role in upregulating myocardial proteasome activities and sustained upregulation of proteasome assembly, thereby assisting in maintaining proteostasis and protecting against maladaptive cardiac remodeling and HF during systolic overload. - Source: PubMed
Ahammed Md SalimWu PenglongWang YifanYang LiuqingSternburg Jack OLi FaqianLiu JinbaoWang Xuejun - Urinary extracellular vesicles (uEVs) are potential biomarkers for renal physiology and disease. Their isolation is challenged by Tamm-Horsfall protein (THP) contamination, particularly in high-speed ultracentrifugation (P100) fractions. Low-speed (P20) fractions contain biologically relevant uEVs, yet their proteomic composition is underexplored. This study evaluates strategies for THP removal to optimize mass spectrometry analysis and characterizes P20 and P100 uEV proteomes and its combination in healthy urine. - Source: PubMed
Publication date: 2026/06/14
Bielopolski DanaMusante LucaMolina HenrikBarrows DouglasUpson SamanthaYang LifangCarrol ThomasTobin Jonathan NKost Rhonda GErdbrügger U - Carbon dots offer excellent physico-chemical properties and biocompatibility for cancer theranostics systems, either as therapeutic agents themselves, or as potential drug carriers. It is, however, postulated that the drug carrier affects the mechanism of action and intracellular target molecules of a drug. Therefore, in the present study, we systematically evaluated protein alterations in HeLa cervical cancer cells after treatment with sulfur-doped carbon dots (S-CDs). Synchrotron Radiation μFTIR spectroscopy and label-free LC-MS/MS proteomics integrated with bioinformatics were used to assess molecular changes. μFTIR revealed a shift and increased intensity of α-helices, indicating structural changes in proteins as a result of the interaction between S-CDs and cells. Proteomic analysis identified 122 statistically significant ( ≤ 0.05) proteins with increased abundance and 61 with decreased abundance following S-CD exposure, many of which possess high α-helix content, consistent with μFTIR findings. Functional analyses showed that up-regulated proteins were enriched in molecular adaptor, transporter, and transcription regulator activities, particularly those involved in RNA metabolism and translation. Down-regulated proteins were dominated by protein-modifying enzymes and cytoskeletal components. Pathway enrichment analysis indicated alterations in mRNA processing, ribosomal pathways, translation factors, aminoacyl-tRNA biosynthesis, and proteasome degradation. Key hub proteins included ribosomal proteins and translation initiation factors. S-CD treatment led to opposite regulation of many proteins compared to their regulation in untreated HeLa cells including down-regulation of ribosomal proteins (RPS27L, RPS19, and RPS5), aminoacyl-tRNA biosynthesis proteins (IARS1, LARS1, and MARS1), and proteasome degradation proteins (PSMD2, PSMD3, and PSMD11), which aligns with the observed cytotoxic effect of S-CDs on cervical cancer cells. Overall, these results highlight significant proteomic and structural protein changes induced by S-CDs and support their potential for cervical cancer treatment, warranting further investigation of this nanomaterial's biological applications. - Source: PubMed
Publication date: 2026/03/26
Davalieva KatarinaRalić VanjaBozhinovski GjorgjiGemović BranislavaNešić Maja DKorićanac LelaDučić TanjaAlgarra ManuelPopović Iva AStepić MilutinPetković Marijana - Bladder cancer (BCa), a highly prevalent and aggressive tumor of the urinary system, typically exhibits poor clinical outcomes, particularly in advanced stages where therapeutic efficacy remains inadequate. A key characteristic of tumorigenesis, metabolic reprogramming, contributes substantially to cancer cell proliferation and metastatic progression. In the current investigation, phosphoglucomutase 3 (PGM3) was markedly overexpressed in BCa tissues, with elevated PGM3 expression strongly associated with unfavorable prognosis. Downregulation of PGM3 inhibited BCa tumor growth and metastasis by suppressing energy metabolism pathways, including glycolysis and oxidative phosphorylation (OXPHOS). Mechanistically, proteasome 26S subunit non-ATPase 11 (PSMD11) interacted with PGM3, reducing its ubiquitination and proteasomal degradation. Additionally, Parkin acted as a ubiquitinase, destabilizing PGM3, whereas PSMD11 competed with Parkin for PGM3 binding, thereby attenuating Parkin-mediated ubiquitination and stabilizing PGM3. Further analysis demonstrated that PSMD11 enhanced glycolysis and OXPHOS through PGM3, promoting BCa malignancy. Higher PSMD11 expression positively correlated with increased PGM3 expression. Collectively, these findings suggest that targeting the PSMD11/PGM3 axis could provide a promising therapeutic strategy for BCa. - Source: PubMed
Publication date: 2026/04/06
Cheng YuChen TaoZheng GuanghaoSong ZhenZhang GanXiao SongRao XuepengZeng Tao