PSMD13: A Potential Drug Target and Biomarker for 26S Proteasome Regulatory Subunit p40.5

Target Name: PSMD13

NCBI ID: G5719

PSMD13

PSMD13: A Potential Drug Target and Biomarker for 26S Proteasome Regulatory Subunit p40.5

Introduction

The 26S proteasome is a key regulatory subunit that plays a crucial role in protein degradation and cell signaling. It is composed of two main subunits, p17 and p40.5, which function together to ensure the proper degradation of protein and maintain cellular homeostasis. The p40.5 subunit has been identified as a potential drug target and biomarker due to its unique structure and functions.

Structure and Functions of PSMD13

PSMD13 is a 26S proteasome regulatory subunit p40.5 that consists of 154 amino acid residues. It has a unique 21-amino acid extension at its C-terminus, which is not found in any other known 26S proteasome subunit. This extension is known as the N-terminal hypervariable region (HVR) and is involved in the formation of a distinct N-terminal region that interacts with the 26S proteasome light chain.

The N-terminal HVR of PSMD13 is rich in conserved secondary structure elements, such as a 尾-sheet, a 纬-helix, and a variable loop, which are important structural features that contribute to the stability and function of the subunit (3 ). Additionally, the HVR region contains a putative nucleotide-binding site (NBS), which is known to play a role in protein-protein interactions.

Expression and Localization

PSMD13 is expressed in a variety of tissues and cells, including muscle, liver, and brain, and its levels vary depending on the cell type and the level of translation. It is predominantly expressed in the cytoplasm, which suggests that it is involved in cytoplasmic protein degradation.

Localization studies have shown that PSMD13 is predominantly located in the endoplasmic reticulum (ER) and is also found in the cytosol, which suggests that it is involved in both intracellular and extracellular protein degradation.

Drug Targeting and Biomarkers

The unique structure and functions of PSMD13 make it an attractive drug target. The N-terminal HVR region has been shown to be involved in protein-protein interactions and can interact with other 26S proteasome subunits, such as p18, via a conserved interface (8 ). This interaction suggests that targeting PSMD13 may be an effective way to modulate the activity of the 26S proteasome and improve protein degradation.

In addition, the HVR region has also been shown to be involved in the formation of the 26S proteasome dimer, which is critical for protein degradation. Therefore, targeting PSMD13 may also be a way to regulate the activity of the 26S proteasome and improve protein degradation in cancer cells.

Biomarker studies have also shown that PSMD13 levels are decreased in various types of cancer, such as colon cancer, breast cancer, and lung cancer, due to its involvement in cell signaling. Therefore, PSMD13 may be a useful biomarker for monitoring the effectiveness of cancer treatments.

Conclusion

PSMD13 is a unique and highly conserved 26S proteasome regulatory subunit that has been identified as a potential drug target due to its unique structure and functions. The N-terminal HVR region has been shown to be involved in protein-protein interactions and can interact with other 26S proteasome subunits. Biomarker studies have also shown that PSMD13 levels are decreased in various types of cancer, making it an attractive target for drug development. Further studies are needed to

Protein Name: Proteasome 26S Subunit, Non-ATPase 13

Functions: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair

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