PSMC4: A Potential Drug Target and Biomarker for Proteasome-Mediated Diseases

Target Name: PSMC4

NCBI ID: G5704

PSMC4

PSMC4: A Potential Drug Target and Biomarker for Proteasome-Mediated Diseases

Proteasomes, also known as proteasomes or simply "proteases", are complex protein structures responsible for breaking down and degrading various proteins in the cell. These highly specific machines play a crucial role in maintaining cellular homeostasis and are involved in various cellular processes, including DNA replication, gene expression, and response to stress. The 26S subunit of the proteasome, as represented by PSMC4, is a key component of this complex machinery that functions essential roles in cellular processes.

The discovery of PSMC4 as a potential drug target and biomarker has significant implications for the development of new therapeutic strategies. In this article, we will explore PSMC4's structure, function, and potential as a drug target, as well as its potential as a biomarker for various diseases.

Structure and Function

PSMC4 is a 26S subunit of the proteasome, which consists of 28 subunits when complete. It is characterized by a distinct N-terminus, a catalytic core, and a C-terminus that is involved in interactions with various substrates. PSMC4 contains several conserved domains, including an ATPase domain (2), a nucleotide-binding oligomerization domain (3), a scaffold domain (4), and a hydrophobic domain.

The ATPase domain is a key component of the PSMC4 structure, as it plays a crucial role in regulating the activity of the proteasome. This domain is responsible for the transfer of ATP to the active site on the protein substrates, which initiates the process of protein degradation. The nucleotide-binding oligomerization domain (NBD) is another conserved domain found in several proteins, including PSMC4. This domain is responsible for binding nucleotides to the protein, which enables the PSMC4 to interact with various nucleotide-containing substrates.

The scaffold domain is a conserved region that is involved in the regulation of protein stability and localization. This domain is known to play a crucial role in the assembly and disassembly of the proteasome complex.

The hydrophobic domain is a conserved region that is involved in the regulation of protein function. This domain is known to play a crucial role in the stability and localization of the PSMC4 protein (1).

Potential as a Drug Target

PSMC4 has been identified as a potential drug target due to its unique structure and function. The PSMC4 protein is involved in various cellular processes, including the regulation of protein degradation and the assembly and disassembly of the proteasome complex. Therefore, blocking the activity of PSMC4 could be an effective strategy for treating diseases that are characterized by the overproduction or underproduction of proteins.

One of the most promising approaches to blocking the activity of PSMC4 is to develop small molecules that specifically inhibit the ATPase domain. These small molecules would be able to bind to the ATPase domain and prevent it from binding ATP, which would inhibit the activity of the PSMC4 protein.

PSMC4 has also been shown to play a role in the regulation of gene expression, which makes it an attractive target for small molecules that aim to modulate cellular gene expression. For example, small molecules that can specifically interact with the PSMC4 protein have been shown to be able to repress the activity of gene transcription factors, thereby inhibiting the translation of mRNAs into protein.

Potential as a Biomarker

PSMC4 has also been shown to serve as a potential biomarker for various diseases. The PSMC4 protein is involved in the regulation of protein degradation, which is a critical process for the diagnosis of diseases characterized by the overproduction or underproduction of proteins, such as neurodegenerative diseases, cancer, and diseases associated with protein misfolding, such as amyloidosis.

In addition to its role in protein degradation, PSMC4 has also been shown to play a role in

Protein Name: Proteasome 26S Subunit, ATPase 4

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. PSMC4 belongs to the heterohexameric ring of AAA (ATPases associated with diverse cellular activities) proteins that unfolds ubiquitinated target proteins that are concurrently translocated into a proteolytic chamber and degraded into peptides

The "PSMC4 Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about PSMC4 comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
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•   the target screening and validation;
•   expression level;
•   disease relevance;
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•   related combination drugs;
•   pharmacochemistry experiments;
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•   advantages and risks of development, etc.
The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

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