Ask about this productRelated genes to: PSMB6 antibody
- Gene:
- PSMB6 NIH gene
- Name:
- proteasome subunit beta 6
- Previous symbol:
- -
- Synonyms:
- Y, DELTA
- Chromosome:
- 17p13.2
- Locus Type:
- gene with protein product
- Date approved:
- 1995-05-03
- Date modifiied:
- 2016-10-05
- Gene:
- PSMB9 NIH gene
- Name:
- proteasome subunit beta 9
- Previous symbol:
- LMP2
- Synonyms:
- RING12, beta1i, PSMB6i
- Chromosome:
- 6p21.32
- Locus Type:
- gene with protein product
- Date approved:
- 1991-12-18
- Date modifiied:
- 2016-10-05
Related products to: PSMB6 antibody
Related articles to: PSMB6 antibody
- The proteasome is a multicatalytic complex responsible for protein degradation and regulation of immune responses, and has been implicated in type 1 diabetes mellitus (T1DM) pathogenesis. Zinc (Zn) is essential for insulin granule biogenesis and modulates proteasomal activity. This study investigated associations between single-nucleotide polymorphisms (SNPs) in proteasomal subunits predicted to bind Zn and T1DM susceptibility or related traits. - Source: PubMed
Publication date: 2025/11/28
Nasre-Nasser Raif GregorioMeireles Vieira Anna CarolinaPellenz Felipe MateusMoretto LucianeGirardi EliandraAssmann Taís SilveiraLu Chih-HaoCanani Luís HenriqueDieter CristineCrispim Daisy - Bortezomib (BTZ)-based regimens play a crucial role in the treatment of multiple myeloma (MM), significantly improving patient outcomes. BTZ, a proteasome inhibitor, interferes with cellular processes essential for cancer cell growth and survival, resulting in high response rates. Its use in initial and recurrent treatment strategies has been associated with extended disease control and improved long-term outcomes, contributing to overall survival. This study aimed to delineate the clinical characteristics of newly diagnosed MM patients and investigate the influence of single nucleotide polymorphisms (SNPs) in and genes on the risk and response to BTZ-based chemotherapy, in comparison with the control group. - Source: PubMed
Publication date: 2025/03/24
Sood NidhiHamide AbdoulDubashi BiswajitJayanthi MathaiyanMunirajan A K - Postmitotic skeletal muscle critically depends on tightly regulated protein degradation to maintain proteomic stability. Impaired macroautophagy/autophagy-lysosomal or ubiquitin-proteasomal protein degradation causes the accumulation of damaged proteins, ultimately accelerating muscle dysfunction with age. While studies have demonstrated the complementary nature of these systems, their interplay at the organism levels remains poorly understood. Here, our study reveals novel insights into this complex relationship in autophagy-deficient skeletal muscle. We demonstrated that despite a compensatory increase in proteasome level in response to autophagy impairment, 26S proteasome activity was not proportionally enhanced in autophagy-deficient skeletal muscle. This functional deficit was partly attributed to reduced ATP levels to fuel the 26S proteasome. Remarkably, we found that activation of EIF4EBP1, a crucial inhibitor of cap-dependent translation, restored and even augmented proteasomal function through dual mechanisms. First, genetically activating EIF4EBP1 enhanced both ATP-dependent 26S proteasome and ATP-independent 20S proteasome activities, thereby expanding overall protein degradation capacity. Second, EIF4EBP1 activation caused muscle fiber transformation and increased mitochondrial biogenesis, thus replenishing ATP levels for 26S proteasome activation. Notably, the improved performance of the 20S proteasome in EIF4EBP1-activated skeletal muscle was attributed to an increased abundance of the immunoproteasome, a subtype specially adapted to function under oxidative stress conditions. This dual action of EIF4EBP1 activation preserved proteomic integrity in autophagy-deficient skeletal muscle. Our findings uncover a novel role of EIF4EBP1 in improving protein quality control, presenting a promising therapeutic strategy for autophagy-related muscular disorders and potentially other conditions characterized by proteostatic imbalance.: 3-MA: 3-methyladenine; ACAC/ACC: acetyl-Coenzyme A carboxylase; AMPK: AMP-activated protein kinase; ATG5: autophagy related 5; ATG7: autophagy related 7; ATP: adenosine triphosphate; ATP5F1A/ATP5A: ATP synthase F1 subunit alpha; CKM-Cre: creatine kinase, muscle-Cre; CMA: chaperone-mediated autophagy; CTSB: cathepsin B; CTSK: cathepsin K; CTSL: cathepsin L; CUL3: cullin 3; EDL: extensor digitorum longus; EIF4E: eukaryotic translation initiation factor 4E; EIF4EBP1: eukaryotic translation initiation factor 4E binding protein 1; EIF4F: eukaryotic translation initiation factor 4F complex; FBXO32/ATROGIN1/MAFbx: F-box protein 32; GFP: green fluorescent protein; IFNG/IFN-γ: interferon gamma; KEAP1: kelch-like ECH-associated protein 1; LAMP1: lysosomal-associated membrane protein 1; LAMP2: lysosomal-associated membrane protein 2; MAP1LC3/LC3: microtubule-associated protein 1 light chain 3; MEF: mouse embryonic fibroblast; -Cre: myosin, light polypeptide 1 (promoter driving Cre recombinase); mRFP: monomeric red fluorescent protein; MTOR: mechanistic target of rapamycin kinase; MTORC1: MTOR complex 1; NFE2L1/NRF1: nuclear factor, erythroid derived 2, like 1; NFE2L2/NRF2: nuclear factor, erythroid derived 2, like 2; NFKB1/NFκB1: nuclear factor of kappa light polypeptide gene enhancer in B cells 1, p105; OXPHOS: oxidative phosphorylation; PPARGC1A/PGC1α: peroxisome proliferator activated receptor, gamma, coactivator 1 alpha; PSMB5: proteasome (prosome, macropain) subunit, beta type 5; PSMB6: proteasome (prosome, macropain) subunit, beta type 6; PSMB7: proteasome (prosome, macropain) subunit, beta type 7; PSMB8: proteasome (prosome, macropain) subunit, beta type 8 (large multifunctional peptidase 7); PSMB9: proteasome (prosome, macropain) subunit, beta type 9 (large multifunctional peptidase 2); PSMB10: proteasome (prosome, macropain) subunit, beta type 10; PSME1: proteasome (prosome, macropain) activator subunit 1 (PA28 alpha); PSME2: proteasome (prosome, macropain) activator subunit 2 (PA28 beta); RBX1: ring-box 1; SQSTM1/p62: sequestosome 1; SREBF1/SREBP1: sterol regulatory element binding transcription factor 1; STAT3: signal transducer and activator of transcription 3; TRIM63/MURF1: tripartite motif-containing 63; ULK1: unc-51 like kinase 1; UPS: ubiquitin-proteasome system. - Source: PubMed
Publication date: 2025/02/06
Dong HanLyu YifanHuang Chien-YungTsai Shih-Yin - Based on the recent evidence of IL-1 inhibition in patients with rheumatoid arthritis (RA) and concomitant type 2 diabetes (T2D), we evaluated the synovial tissue expression of IL-1 related genes in relationship to the ubiquitin-proteasome system and the effects of insulin on ubiquitinated proteins in fibroblast-like synoviocytes (FLSs). - Source: PubMed
Publication date: 2024/09/28
Ruscitti PieroCurrado DamianoRivellese FeliceVomero MartaNavarini LucaCipriani PaolaPitzalis CostantinoGiacomelli Roberto - The ubiquitin/proteasome system (UPS) plays a crucial role in maintaining cellular protein homeostasis. The catalytic activity of proteasome in the UPS is regulated by β1 (PSMB6), β2 (PSMB7), and β5 (PSMB5) subunits. Interferon (IFN)-γ, tumor necrosis factor (TNF)-α, inflammation, and oxidative stress can induce the replacement of β1, β2, and β5 with their respective immuno-subunits β1i (PSMB9), β2i (PSMB10), and β5i (PSMB8), which can be assembled into the immunoproteasome. Compared with the standard proteasome, the immunoproteasome exerts enhanced regulatory effects on immune responses, such as processing and presenting MHC class Ⅰ antigens, production of pro-inflammatory cytokines, and T cell differentiation and proliferation. Abnormal aggregation of immunoproteasomes can cause neurodegenerative diseases like Parkinson's disease, Alzheimer's disease, and amyotrophic lateral sclerosis. To explore the function of PSMB9 after bacterial infection, we constructed a lentivirus plasmid overexpressing PSMB9-eGFP-His and transfected the plasmid into HEK293T cells for packaging by using a triple-plasmid system in this study. After screening with puromycin, we obtained a stable human leukemia monocytic THP-1 cell line expressing the fusion protein of PSMB9. Western blotting (WB) and fluorescence microscopy verified the expression of the fusion protein in the stable THP-1 cells. Quantitative PCR (qPCR) was employed to measure the copies of - in THP-1 cells. Immunofluorescence results found that eGFP-His did not affect the subcellular localization of PSMB9. The purification with nickel affinity chromatography confirmed that the fusion protein could be assembled into the 20S immunoproteasome and exhibited cleaving activity for fluorescent peptide substrates. These results indicated that the - fusion gene was integrated into the chromosome, and could be stably expressed in the constructed THP-1 cell line. This cell line can be utilized for the research on subcellular localization, dynamic expression, and activity of PSMB9 in live cells at different infection conditions and disease stages. It also provides a model for the stable cell lines construction of other immunoproteasome subunits PSMB8 and PSMB10. - Source: PubMed
Wang JiahaoFeng LijieZhang YaoXu Ping