Psma1, the proteasome subunit alpha type 1, is a component of the 26S proteasome, a cellular protein degradation complex [3]. The ubiquitin-proteasome system, in which Psma1 is involved, regulates substrate-specific proteolysis during various biological processes such as the cell cycle, apoptosis, and fertilization, and is also associated with pathologies like Alzheimer's disease, cancer, and liver cirrhosis [6].

In cancer research, studies have shown that Psma1 is upregulated in multiple cancers. In gastric carcinoma, it promotes tumor progression and proliferation by deubiquitinating and stabilizing TAZ, a downstream gene [1]. In lung squamous cell carcinoma, knockdown of Psma1 significantly decreased cell proliferation and promoted apoptosis, indicating its role in tumor growth [2]. In oral squamous cell carcinoma, its overexpression correlated with advanced clinicopathological features and poorer prognosis [3]. In glioblastoma multiforme, a lncRNA MDHDH binds to Psma1 and MDH2, accelerating the degradation of MDH2 and affecting mitochondrial function and NAD + metabolism [5]. In the context of autoimmune podocytopathies, serum anti-Psma1 autoantibodies are elevated in the active phase of idiopathic nephrotic syndrome, and Psma1 plays an important role in maintaining podocyte morphology and function [4].

In conclusion, Psma1 is crucial for protein degradation processes in normal biological functions. Its dysregulation is associated with various diseases, especially cancers. Research on Psma1, including through gene-based models, has provided insights into its role in disease development, offering potential therapeutic targets for cancer treatment and biomarkers for disease diagnosis and prognosis [1,2,3,4,5].