Proteosomin

Proteosomin is a protein complex involved in the degradation of misfolded proteins in the cell. It was first identified in the context of neurodegenerative diseases, where it plays a crucial role in the clearance of aggregated proteins. The proteosomin complex consists of at least 14 subunits, including the proteasome activator subunit 1 (PA28), which is essential for its activity. The complex is recruited to protein aggregates through its interaction with chaperone proteins, such as heat shock protein 70 (Hsp70) and heat shock protein 40 (Hsp40). Once recruited, the proteosomin complex facilitates the unfolding of the aggregated proteins, making them accessible for degradation by the proteasome. This process is vital for maintaining cellular homeostasis and preventing the accumulation of toxic protein aggregates, which are associated with various diseases, including Alzheimer's, Parkinson's, and Huntington's diseases. The proteosomin complex has emerged as a promising target for therapeutic interventions aimed at treating these neurodegenerative disorders.