Prefoldin (PFDN) is a hexameric chaperone complex that is widely found in eukaryotes and archaea and consists of six different subunits (PFDN1-6). Its main function is to transfer actin and
tubulin monomers to the eukaryotic cell cytoplasmic chaperone
protein (c-CPN) specific binding during the assembly of the cytoskeleton, to stabilize the newly synthesized
peptides so that they can be folded correctly. The current study found that each subunit of PFDN has different functions, which are closely related to the occurrence, development and prognosis of
tumors. However, the best characteristics of each subunit have not been fully affirmed. The connection between research and
tumors can change the understanding of PFDN and further extend its potential prognostic role and structural function to
cancer research and clinical practice. This article mainly reviews the role of canonical PFDN and its subunits in
tumors and other diseases, and discusses the potential prospects of the unique structure and function of PFDN in nanomedicine.