PSME1

Last update 08 May 2025

Basic Info

Synonyms

11S regulator complex subunit alpha, Activator of multicatalytic protease subunit 1, IFI5111

+ [9]

Introduction

Implicated in immunoproteasome assembly and required for efficient antigen processing. The PA28 activator complex enhances the generation of class I binding peptides by altering the cleavage pattern of the proteasome.

100 Clinical Results associated with PSME1

100 Translational Medicine associated with PSME1

0 Patents (Medical) associated with PSME1

126

Literatures (Medical) associated with PSME1

01 Nov 2024·Genes & Diseases

The proteasome activator subunit PSME1 promotes HBV replication by inhibiting the degradation of HBV core protein

Article

Author: Yang, Jiaxin ; Liu, Yu ; Fan, Hui ; Zeng, Qiqi ; Huang, Ailong ; Fan, Yao ; Wang, Yanyan

Chronic hepatitis B virus (HBV) infection is a leading cause of liver cirrhosis and hepatocellular carcinoma, representing a global health problem for which a functional cure is difficult to achieve. The HBV core protein (HBc) is essential for multiple steps in the viral life cycle. It is the building block of the nucleocapsid in which viral DNA reverse transcription occurs, and its mediation role in viral-host cell interactions is critical to HBV infection persistence. However, systematic studies targeting HBc-interacting proteins remain lacking. Here, we combined HBc with the APEX2 to systematically identify HBc-related host proteins in living cells. Using functional screening, we confirmed that proteasome activator subunit 1 (PSME1) is a potent HBV-associated host factor. PSME1 expression was up-regulated upon HBV infection, and the protein level of HBc decreased after PSME1 knockdown. Mechanistically, the interaction between PSME1 and HBc inhibited the degradation of HBc by the 26S proteasome, thereby improving the stability of the HBc protein. Furthermore, PSME1 silencing inhibits HBV transcription in the HBV infection system. Our findings reveal an important mechanism by which PSME1 regulates HBc proteins and may facilitate the development of new antiviral therapies targeting PSME1 function.

01 Jun 2024·Cancer Medicine

Obesity enhances the response to neoadjuvant anti‐PD1 therapy in oral tongue squamous cell carcinoma

Article

Author: Chen, Yanfeng ; Li, Guoli ; Tan, Xiyan ; Wang, Yaqin ; Xiao, Guoming ; Deng, Honghao ; Zhang, Chenzhi

AbstractObjectivesPrevious studies have demonstrated that obesity may impact the efficacy of anti‐PD1 therapy, but the underlying mechanism remains unclear. In this study, our objective was to determine the prognostic value of obesity in patients with oral tongue squamous cell carcinoma (OTSCC) treated with pembrolizumab and establish a subtype based on fatty acid metabolism‐related genes (FAMRGs) for immunotherapy.Materials and MethodsWe enrolled a total of 56 patients with OTSCC who underwent neoadjuvant anti‐PD1 therapy. Univariate and multivariate Cox regression analyses, Kaplan–Meier survival analysis, and immunohistochemistry staining were performed. Additionally, we acquired the gene expression profiles of pan‐cancer samples and conducted GSEA and KEGG pathway analysis. Moreover, data from TCGA, MSigDB, UALCAN, GEPIA and TIMER were utilized to construct the FAMRGs subtype.ResultsOur findings indicate that high Body Mass Index (BMI) was significantly associated with improved PFS (HR = 0.015; 95% CI, 0.001 to 0.477; p = 0.015), potentially attributed to increased infiltration of PD1 + T cells. A total of 91 differentially expressed FAMRGs were identified between the response and non‐response groups in pan‐cancer patients treated with immunotherapy. Of these, 6 hub FAMRGs (ACSL5, PLA2G2D, PROCA1, IL4I1, UBE2L6 and PSME1) were found to affect PD‐1 expression and T cell infiltration in HNSCC, which may impact the efficacy of anti‐PD1 therapy.ConclusionThis study demonstrates that obesity serves as a robust prognostic predictor for patients with OTSCC undergoing neoadjuvant anti‐PD1 therapy. Furthermore, the expression of 6 hub FAMRGs (ACSL5, PLA2G2D, PROCA1, IL4I1, UBE2L6 and PSME1) plays a pivotal role in the context of anti‐PD1 therapy and deserves further investigation.

01 Sep 2023·International Immunopharmacology

Proteomics profiling of CD4 + T-cell-derived exosomes from patients with rheumatoid arthritis

Article

Author: Huang, Lixin ; Huang, Zhixiang ; Chen, Jiajun ; Huang, Yukai ; Ji, Zhuyi ; Huang, Qidang ; Li, Tianwang ; Sun, Shanmiao ; Chen, Shuyang ; Liu, Meng ; Deng, Weiming ; Liang, Ling ; Huang, Xuechan ; Zheng, Shaoling ; Ding, Jiali

OBJECTIVESOur study profiled the CD4 + T-cell-derived exosomes from patients with rheumatoid arthritis (RA) using proteomics.METHODSProteomic analysis of CD4 + T-cell-derived exosomes was performed by tandem mass tags (TMT) combined with LC-MS/MS. We validated the most significantly upregulated and downregulated proteins using ELISA and WB.RESULTSThe proteomic results showed that there were 3 upregulated differentially expressed proteins and 31 downregulated differentially expressed proteins in the RA group. The results indicated that dihydropyrimidinase-related protein 3 (DPYSL3) was significantly upregulated in CD4 + T-cell-derived exosomes, whereas proteasome activator complex subunit 1 (PSME1) was significantly downregulated in the RA group. Bioinformatics analysis showed that proteins were enriched in "positive regulation of gene expression", "antigen processing and presentation", "acute-phase response" and "PI3K-AKT signaling" pathways. ELISA verified that compared to the control group, the RA group showed significant upregulation of DPYSL3, and downregulation of PSME1 in CD4 + T-cell-derived exosomes.CONCLUSIONSThe proteomic analysis results of CD4 + T-cell-derived exosomes from patients with RA suggest that these differentially expressed proteins may be involved in RA pathogenesis. DPYSL3 and PSME1 may become useful biomarkers for RA.

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PSME1

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