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Prefoldin subunit 1 is a protein encoded by the PFDN1 gene. It is one of six subunits (four beta, two alpha) that form the prefoldin complex, a molecular chaperone critical for capturing and stabilizing newly synthesized polypeptide chains, preventing their aggregation and misfolding. Prefoldin primarily binds unfolded actin and tubulin, transferring them to the TRiC/CCT chaperonin complex for proper folding. This activity is ATP-independent and central to cytoskeletal protein homeostasis. Beyond cytoplasmic roles, prefoldin subunits also participate in transcriptional regulation and the proteasome-mediated degradation of proteins. Disruption of prefoldin function is linked to neurodegenerative disorders, cancer, and rare mitochondrial diseases. PFDN1 and the prefoldin complex are increasingly studied as potential therapeutic targets and biomarkers for diseases involving impaired protein folding and cellular stress responses[1][2][3][4][5].
Stabilization and transfer of unfolded polypeptides to chaperonin complexes for folding; Prevention of protein misfolding and aggregation
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