PSMD14: A promising drug target for the treatment of neurodegenerative diseases

Target Name: PSMD14

NCBI ID: G10213

PSMD14

PSMD14: A promising drug target for the treatment of neurodegenerative diseases

Proteasomes, also known as proteomes, are complex protein structures that play a crucial role in cellular homeostasis and are involved in various cellular processes, including DNA replication, protein degradation, and stress responses. The 26S subunit of the proteasome, named PSMD14, has been identified as a promising drug target for the treatment of neurodegenerative diseases due to its unique structure and function.

Structure and function of PSMD14

PSMD14 is a non-ATPase protein that belongs to the family of ubiquitin-like proteins (UCPs). It has a unique 14-amino acid residue at its N-terminus, which is unusual for a protein of its size and function. PSMD14 has a molecular weight of approximately 18 kDa and a pre-folding length of 13 amino acids.

PSMD14 functions as a key component of the proteasome machinery by helping to promote the formation of the 26S subunit. The 26S subunit is the most abundant subunit of the proteasome and is responsible for the degradation of proteins in the cytosol. PSMD14 plays a vital role in this process by interacting with the 26S subunit and helping to establish a stable complex between the two subunits.

PSMD14 is also involved in the regulation of protein stability and in the detoxification of damaged proteins. It has been shown to interact with various protein substrates and to play a role in the detoxification of foreign particles, such as viruses and bacteria, in the cytosol.

Drug targeting of PSMD14

The unique structure and function of PSMD14 make it an attractive drug target for the treatment of neurodegenerative diseases. Several studies have shown that blocking PSMD14 activity can lead to the degradation of damaged proteins and improve the survival of neurodegenerate animals.

One of the most promising strategies for targeting PSMD14 is the use of small molecules, such as inhibitors or modulators of the proteasome. Several inhibitors have been shown to specifically target PSMD14 and to display neuroprotective effects in animal models of neurodegenerative diseases.

Another approach for targeting PSMD14 is the use of antibodies that can specifically recognize and label PSMD14. This approach has been shown to be effective in blocking the activity of PSMD14 in neurodegenerate models and in improving the survival of neurodegenerate animals.

Conclusion

PSMD14 is a non-ATPase protein that plays a crucial role in the regulation of protein stability and in the detoxification of damaged proteins. Its unique structure and function make it an attractive drug target for the treatment of neurodegenerative diseases. Several studies have shown that blocking PSMD14 activity can lead to the degradation of damaged proteins and improve the survival of neurodegenerate animals. Further research is needed to develop more effective and specific inhibitors or modulators of PSMD14 for the treatment of neurodegenerative diseases.

Protein Name: Proteasome 26S Subunit, Non-ATPase 14

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. The PSMD14 subunit is a metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains within the complex. Plays a role in response to double-strand breaks (DSBs): acts as a regulator of non-homologous end joining (NHEJ) by cleaving 'Lys-63'-linked polyubiquitin, thereby promoting retention of JMJD2A/KDM4A on chromatin and restricting TP53BP1 accumulation. Also involved in homologous recombination repair by promoting RAD51 loading

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