The 26S proteasome is a crucial component of the ubiquitin-proteasome system (UPS), responsible for the degradation of ubiquitinated proteins in an ATP-dependent manner. This system plays a vital role in maintaining cellular homeostasis by removing misfolded, damaged, or unneeded proteins. The 26S proteasome is composed of a 20S core particle (CP) and two 19S regulatory particles (RP). The regulatory particle is further divided into a base and a lid, with the lid containing several non-ATPase subunits, including the 26S proteasome non-ATPase regulatory subunit 11 (PSMD11) .
PSMD11, also known as Rpn6, S9, or p44.5, is a non-ATPase subunit of the 19S regulatory particle of the 26S proteasome. It is encoded by the PSMD11 gene located on chromosome 17 in humans and chromosome 11 in mice . PSMD11 is a member of the proteasome subunit S9 family and is phosphorylated by AMP-activated protein kinase (AMPK) .
The primary function of PSMD11 is to regulate the proteasome’s activity by participating in the assembly and stability of the 19S regulatory particle. It plays a key role in the ATP-dependent degradation of ubiquitinated proteins, which is essential for various cellular processes, including cell cycle regulation, signal transduction, and stress responses .
The 26S proteasome, including PSMD11, is distributed throughout eukaryotic cells at high concentrations. It cleaves peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. This process is crucial for maintaining protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions and by degrading proteins whose functions are no longer required .
Mouse anti-human PSMD11 antibodies are commonly used in research to study the function and regulation of the 26S proteasome. These antibodies can be used in various applications, including Western blotting, immunoprecipitation, and immunofluorescence, to detect and quantify PSMD11 expression in human cells. They are valuable tools for investigating the role of PSMD11 in cellular processes and disease mechanisms .