Molecular Weight:
Domains: Forms a heterohexameric ring structure with PSME2 (PA28β) as part of the 11S proteasome activator (PA28) .
Recombinant PSME1 is typically expressed in Escherichia coli with >90% purity, enabling use in SDS-PAGE, mass spectrometry, and immunoproteasome studies .
Enhances proteasome cleavage efficiency to generate antigenic peptides for MHC class I presentation .
Induced by interferon-γ, facilitating immune response coordination .
Gene | Median Survival (Days) | Hazard Ratio (95% CI) |
---|---|---|
PSME1 | 3,136 (high) vs. 2,030 (low) | 0.685 (0.516–0.910) |
PSME2 | 3,379 (high) vs. 1,917 (low) | 0.576 (0.431–0.769) |
In vivo studies show PSME1-specific antibody accumulation in prostate xenografts, highlighting its accessibility as a therapeutic target .
PSME1 exhibits broad tissue distribution with elevated expression in immune-rich organs:
REG-alpha, PA28alpha, PA28a, Proteasome Activator subunit-1, Proteasome Activator 28 subunit alpha.
What technical hurdles arise when quantifying PSME1 in heterogeneous samples?
How do PSME1 polymorphisms or isoforms affect experimental outcomes?
Can PSME1 serve as a multi-disease biomarker?
Evidence Table:
What computational tools are suited for PSME1 pathway analysis?
Does PSME1 interact with immune checkpoint regulators?
Preliminary data suggest PSME1-high gastric tumors have elevated PD-1/CTLA-4 expression and higher tumor mutational burden (TMB), making them candidates for immunotherapy .
How does PSME1 influence non-cancer pathologies (e.g., metabolic diseases)?
Proteasome Activator Subunit 1 (PA28α), also known as PSME1, is a protein encoded by the PSME1 gene in humans. This protein plays a crucial role in the regulation of the proteasome, a complex responsible for degrading unneeded or damaged proteins by proteolysis, a chemical reaction that breaks peptide bonds.
The proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of two complexes: a 20S core and a 19S regulator. The 20S core is made up of four rings of 28 non-identical subunits, while the 19S regulator consists of a base with six ATPase subunits and two non-ATPase subunits, and a lid with up to ten non-ATPase subunits .
PA28α is a subunit of the 11S regulator, also known as the PA28 activator complex. This complex enhances the generation of class I binding peptides by altering the cleavage pattern of the proteasome, which is essential for efficient antigen processing . The 11S regulator replaces the 19S regulator in the immunoproteasome, a modified proteasome involved in the processing of class I MHC peptides .
High expression of PA28α has been associated with poor survival in patients with soft tissue leiomyosarcomas, a type of cancer. Studies have shown that high nuclear expression of PA28α predicts poor survival and decreased metastasis-free survival in these patients . This makes PA28α a potential prognostic biomarker for certain types of cancer.