CCT8 (chaperonin containing TCP1 subunit 8) is an essential component of the TRiC/CCT chaperonin complex that assists in protein folding of approximately 10% of the cellular proteome, including actin and tubulin, through ATP hydrolysis 1. The TRiC complex assembles through a hierarchical pathway where CCT8, along with CCT1, CCT3, and CCT6, comprises the positively charged hemisphere that binds unfolded actin more strongly and joins the ring individually during late assembly stages 2. Beyond its canonical chaperone function, CCT8 exhibits significant oncogenic properties across multiple cancer types. It is overexpressed in gliomas, where it regulates proliferation, invasion, and cytoskeletal dynamics 3. In colorectal cancer, CCT8 drives progression through the RPL4-MDM2-p53 axis, contributing to p53 degradation 4. In lung adenocarcinoma, CCT8 promotes metastasis by interacting with and activating AKT signaling pathways 5. CCT8 also supports folding of other proteins like THOC3 in lung cancer progression 6. Remarkably, ectopic CCT8 expression enhances TRiC/CCT complex assembly, prevents protein aggregation, and extends lifespan in C. elegans while maintaining proteostasis 1. Additionally, CCT8 serves as a pro-viral factor during enterovirus infections, facilitating virus morphogenesis through chaperone recruitment 7.