Unlocking the Potential of PSMA7 as a Drug Target and Biomarker

Target Name: PSMA7

NCBI ID: G5688

PSMA7

Unlocking the Potential of PSMA7 as a Drug Target and Biomarker

Proteasome subunit alpha 4 (PSMA7) is a protein that plays a crucial role in the regulation of cell processes, including protein degradation and autophagy. It is also involved in the formation of the endoplasmic reticulum (ER), which is responsible for the delivery of proteins for degradation and storage. PSMA7 has been identified as a potential drug target and biomarker due to its unique structure and various functions in cell signaling pathways.

PSMA7: A Protein Lining the Edge of Protein Trafficking

PSMA7 is a 21-kDa protein that consists of 156 amino acid residues. It is highly conserved, with a calculated pI of 4.87 and a predicted localization in the ER. The ER is a specialized organelle that plays a vital role in the folding and processing of proteins, as well as the degradation of damaged or unnecessary proteins. The ER-associated degradation (ERAD) pathway is a well-established mechanism that involves the targeted removal of damaged or misfolded proteins from the ER. PSMA7 is involved in this process by helping to transport damaged proteins to the ER for degradation.

PSMA7's Role in ER-Associated Degradation

ERAD is a complex process that involves the formation of a protein-protein interaction (PPI) complex in the ER. The PPI is formed by the interaction of the protein transporter (TIR) with its associated protein, which in this case is PSMA7. Once the PPI is formed, it can facilitate the transfer of damaged or misfolded proteins to the ER for degradation.

PSMA7's unique structure and its involvement in the ER-associated degradation pathway make it an attractive drug target. By targeting PSMA7, researchers can potentially disrupt the ER-associated degradation pathway and improve the levels of proteins that are targeted for degradation. This could have therapeutic implications for various diseases, including neurodegenerative disorders, where the ER-associated degradation pathway is disrupted, leading to the accumulation of damaged or misfolded proteins.

PSMA7 as a Biomarker

PSMA7 can also serve as a biomarker for various diseases. The ER-associated degradation pathway is affected in various diseases, including neurodegenerative disorders, where the accumulation of damaged or misfolded proteins is thought to contribute to the development and progression of these disorders. Therefore, the levels of PSMA7 in brain or peripheral tissues can be used as a biomarker for neurodegenerative diseases.

PSMA7 has also been used as a biomarker for cancer, where the ER-associated degradation pathway is disrupted in various types of cancer. The levels of PSMA7 in cancer tissues can be used to monitor the effectiveness of anti-cancer drugs and to identify potential drug targets.

PSMA7 as a Drug Target

PSMA7 is a potential drug target due to its unique structure and its involvement in the ER-associated degradation pathway. By targeting PSMA7, researchers can potentially disrupt the ER-associated degradation pathway and improve the levels of proteins that are targeted for degradation. This could have therapeutic implications for various diseases, including neurodegenerative disorders and cancer.

PSMA7 has been shown to be involved in the formation of the ER-associated degradation pathway in various types of cells. For example, PSMA7 has been shown to play a role in the regulation of protein synthesis and degradation in neuroblasts. It has also been shown to be involved in the regulation of protein export from the ER in various types of cells, including cancer cells.

In addition to its involvement in the ER-associated degradation pathway, PSMA7 has also been shown to have various other functions in cell signaling pathways. For example, PSMA7 has been shown to be involved in the regulation of cell

Protein Name: Proteasome 20S Subunit Alpha 7

Functions: Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). Inhibits the transactivation function of HIF-1A under both normoxic and hypoxia-mimicking conditions. The interaction with EMAP2 increases the proteasome-mediated HIF-1A degradation under the hypoxic conditions. Plays a role in hepatitis C virus internal ribosome entry site-mediated translation. Mediates nuclear translocation of the androgen receptor (AR) and thereby enhances androgen-mediated transactivation. Promotes MAVS degradation and thereby negatively regulates MAVS-mediated innate immune response

The "PSMA7 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 PSMA7 comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
•   its importance;
•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   related combination drugs;
•   pharmacochemistry experiments;
•   related patent analysis;
•   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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