CCT5 (chaperonin containing TCP1 subunit 5) is a core component of the TRiC/CCT chaperonin complex, an eight-subunit molecular machine that facilitates ATP-dependent protein folding 1. Within TRiC, CCT5 assists in folding actin, tubulin, and other cytoplasmic proteins, and contributes to folding WRAP53/TCAB1 to regulate telomere maintenance 2. CCT5 forms part of the negatively charged hemisphere of the TRiC chamber and participates in hierarchical assembly of the complex 2. Loss-of-function mutations in CCT5 cause autosomal recessive hereditary sensory neuropathy with spastic paraplegia, a neurological disorder characterized by lower limb weakness and axonal degeneration 3. A His147Arg mutation in CCT5 impairs hexadecamer assembly and reduces ATPase activity, compromising the chaperone's protein homeostasis functions 4. Beyond neurological disease, CCT5 is upregulated in gastric cancer, where it promotes epithelial-mesenchymal transition and lymph node metastasis by binding E-cadherin and releasing β-catenin to activate Wnt signaling 5. Pan-cancer analysis reveals CCT5 overexpression correlates with poor prognosis across multiple tumor types, suggesting its potential as a biomarker and therapeutic target 6.