Ask about this productRelated genes to: PSMD9 antibody
- Gene:
- PSMD9 NIH gene
- Name:
- proteasome 26S subunit, non-ATPase 9
- Previous symbol:
- -
- Synonyms:
- p27, Rpn4
- Chromosome:
- 12q24.31
- Locus Type:
- gene with protein product
- Date approved:
- 1997-02-19
- Date modifiied:
- 2016-10-05
Related products to: PSMD9 antibody
Related articles to: PSMD9 antibody
- Early detection of Alzheimer's disease (AD) is critical for preventing disease progression. Blood platelets have emerged as a useful peripheral source for AD diagnosis. However, the identification of proteomics-based platelet biomarkers of mild cognitive impairment (MCI) and AD in relation to amyloid β (Aβ) deposition remains largely unexplored. In this study, we compared four groups from 18 participants: subjective memory impairment (SMI, n = 4) as cognitive normal controls, MCI without Aβ deposition (MCI-A(+), n = 5), MCI with Aβ deposition (MCI-A(-), n = 5), and AD (n = 4). We conducted in-depth platelet protein profiling using high-throughput LC-MS/MS with tandem mass tag labeling. Among the total 4,524 proteins detected, we identified both unique and overlapping differentially expressed proteins in MCI-A(+), MCI-A(-), and AD compared with SMI. Hierarchical clustering analysis revealed seven distinct patterns of proteomic alterations across groups. Functional network and gene ontology enrichment analyses indicated that each cluster was associated with specific processes, including platelet activation, AD, and apoptotic signaling pathways. Notably, upregulated proteins in MCI-A(-) and AD were linked to endomembrane system organization. Furthermore, we quantified the relative abundance of multiple protein candidates that were significantly altered in MCI-A(-) and AD compared with SMI and MCI-A(+). Our findings highlight several platelet proteins-ATP6V0C, AP4B1, RAB2B, PSMD9, FKBP1B, and mTOR-as potential molecular targets for predicting AD at the stage of MCI with Aβ deposition, providing new insights into amyloid-related neurodegeneration. - Source: PubMed
Publication date: 2026/03/28
Cho Yeong EunKim AndrewLee Hyeong MinOh Jae WonSon Sang JoonRoh Hyun WoongJung Yi-SookHong Chang HyungLee Sang YoonKim Kwang Pyo - PSMD9/Nas2/Bridge-1 is one of the assembly chaperones of the 19S regulatory particle of the eukaryotic proteasome. While this is among PSMD9's well-recognized roles, the role of PSMD9 in cancer proteasome assembly/disassembly and activity, as a key factor in the ubiquitination and degradation of proteins by the proteasome, unfolded protein response, and proteostasis, nucleolar organization, are some of the recent findings. Several unbiased screening, high-throughput studies, genome-wide association studies (GWAS) have found surprising associations and potential roles for PSMD9 in a variety of diseases or conditions. Although in a majority of these cases the mechanism remains unclear, it is important to take note that this multi-functional protein, in the absence of any enzymatic role, relies primarily on its ability to interact with other proteins and biomolecules in the cells. A surprising range of proteins that associate with PSMD9 discovered by the structure-guided approaches overlaps with many different functions associated with this protein or the proteasome in literature. Collective evidence also points to the possibility that PSMD9 could be an Achilles' heel in some of the solid cancers. - Source: PubMed
Sundararajan RangapriyaHarish MahalakshmiCherusserikkaran Anthony MerlynChristie JoelJaiswal DaminiVenkatraman Prasanna - Osteosarcopenia, defined by the coexistence of osteoporosis and sarcopenia, presents a significant health challenge for aging populations. The purpose of current study was to identify potential therapeutic targets for osteosarcopenia using integrative analysis methods, including multi-omics Mendelian Randomization (MR) and single-cell RNA sequencing (scRNA-seq). - Source: PubMed
Yang JiyongGong MiaolingZhou YiZhao JifengChen WeijianLiu Wengang - Toxic polyglutamine (polyQ) expansions in ataxin-2 (ATXN2) trigger neurodegenerative processes, causing spinocerebellar ataxia type 2, and enhancing TAR DNA-binding protein 43-dependent pathology in amyotrophic lateral sclerosis/frontotemporal dementia. Primary disease events can be compensated transiently, delaying disease manifestation. To define potential therapy targets, here we studied how cells modify phosphoprotein signals, using preferentially affected nervous tissue from end-stage Atxn2-CAG100-Knockin mice. The spinal cord phosphoproteome revealed massive hyperphosphorylations flanking the polyQ expansion in ATXN2 and for SQSTM1 and moderate hyperphosphorylations also for amyotrophic lateral sclerosis proteins, OPTN (optineurin), UBQLN2 (ubiquilin-2), TNIP1 (TNFAIP3 interacting protein 1), and TBK1-targeted TAX1BP1. Conversely, strong hypophosphorylations of WNK1 (protein kinase with no lysine 1), SPARCL1 (secreted protein acidic and cysteine rich-like 1), and PSMD9 (proteasome 19S regulator non-ATPase assembly chaperone P27) were found. Significant enrichments of SRC-homology domain type 3-containing proteins, autophagy/endocytosis factors, and actin modulators could be explained by N-terminal, polyQ-adjacent, proline-rich motifs in ATXN2, suggesting that spinocerebellar ataxia type 2 pathogenesis is highly similar to Huntington's disease, where neurotoxicity is mediated by abnormal polyQ-proline-rich motif-SRC-homology domain type 3 interactions. Validation of protein and mRNA levels was done in mouse spinal cord and embryonic fibroblasts or patient fibroblasts after bafilomycin or arsenite treatment, observing polyQ-dependent OPTN deficiency and SQSTM1 induction impairment. Overall, this phosphoproteome profile identified and quantified the main cellular efforts in adapting autophagy pathways to the aggregation propensity of the ATXN2-N-term. - Source: PubMed
Publication date: 2025/09/22
Almaguer-Mederos Luis-EnriqueKandi Arvind ReddySen Nesli-EceCanet-Pons JúliaBerger Luca-MalenaStokes Matthew PAbell KathrynKey JanaGispert SuzanaAuburger Georg - Understanding protein-protein interactions in cancer is essential for the development of innovative therapeutic strategies. Chaperone proteins often form cooperative networks that regulate key cellular processes, many of which are disrupted in cancer, offering potential targets for intervention. PSMD9, a chaperone involved in 26S proteasome assembly, is frequently overexpressed in various cancers and is linked to resistance to chemotherapy and radiotherapy. It also plays roles in intracellular signaling. Mass spectrometry analysis of proteins co-purified with PSMD9 revealed a subset containing a specific EXKK motif, suggesting potential direct interactions. Among these was DNAJA1, a chaperone involved in mitochondrial protein transport. This study explores and characterizes the interaction between PSMD9 and DNAJA1. The interaction was confirmed through in vitro binding assays using purified proteins and further validated by introducing mutations in DNAJA1 that disrupted the binding. Co-immunoprecipitation from MCF7 breast cancer cells supported the in-cell interaction. Upon proteasomal inhibition, interaction between PSMD9 and DNAJA1 was enhanced in MCF7 cells, correlating with increased DNAJA1 stability. Additionally, PSMD9 depletion led to elevated mitochondrial membrane potential, linking this interaction to mitochondrial regulation. Thus, beyond its known role in cytoplasmic proteostasis, PSMD9 may influence mitochondrial homeostasis via DNAJA1. - Source: PubMed
Publication date: 2025/05/19
Merlyn Anthony CHarish MahalakshmiChristie JoelVenkatraman Prasanna