Prefoldin subunit 5 (PFDN5)

Prefoldin subunit 5 (PFDN5) is one of six subunits comprising the prefoldin complex, a molecular chaperone essential for the folding of nascent proteins, especially tubulin and actin, thus supporting cytoskeletal assembly and maintenance[1][2][4][8]. The complex includes two alpha subunits (including PFDN5) and four beta subunits, assembling into a jellyfish-like heterohexamer that stabilizes and transports unfolded polypeptides to the chaperonin-containing TCP1 complex (CCT) for final folding[4]. Beyond its canonical chaperone role, PFDN5 (also known as Myc modulator 1, MM-1) inhibits transcriptional activity of the proto-oncogene c-Myc and its dysfunction has been implicated in cancer and neurodegenerative conditions[7]. Animal and cellular models show that PFDN5 deficiency disrupts protein homeostasis, induces cytoskeletal abnormalities, increases susceptibility to protein aggregation, and can trigger cell death in tissues with high demands for cytoskeletal proteins or proteostasis[1][6][8]. No approved therapeutic drugs directly target PFDN5, nor is it a classical therapeutic target such as a receptor or enzyme.

Other names

MM-1Myc modulator 1c-Myc-binding protein Mm-1PFD5MM1c-myc binding proteinmyc modulator-1