| Summary: | Shao-jian Mo,1 Hai-Chao Zhao,1 Yan-zhang Tian,2 Hao-Liang Zhao2 1Department of General Surgery, The Affiliated Bethune Hospital of Shanxi Medical University, Taiyuan 030032, People’s Republic of China; 2Department of General Surgery, Shanxi Bethune Hospital, Shanxi Academy of Medical Sciences, Taiyuan 030032, People’s Republic of ChinaCorrespondence: Yan-zhang TianDepartment of General Surgery, Shanxi Bethune Hospital, Shanxi Academy of Medical Sciences, Taiyuan 030032, People’s Republic of ChinaEmail tyz2030@163.comAbstract: 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.Keywords: prefoldin, disease, tumor, nanomedicine
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