CCT3 is a subunit of the chaperonin-containing T-complex (TRiC), a molecular chaperone that assists protein folding upon ATP hydrolysis 1. The TRiC complex mediates folding of cytoskeletal proteins including actin and tubulin, with CCT3 being part of the positively charged chamber hemisphere that binds unfolded actin more strongly 1. TRiC assembly follows a hierarchical pathway where CCT3 joins individually as a late-assembling subunit 1. Beyond its canonical chaperone function, CCT3 has emerged as an important oncogene across multiple cancers. In hepatocellular carcinoma, CCT3 promotes sorafenib resistance by interacting with ACTN4 to inhibit iron endocytosis and prevent ferroptosis 2. CCT3 also acts upstream of YAP and TFCP2 signaling pathways, prolonging their half-life by blocking PCBP2-mediated ubiquitination 3. In lung adenocarcinoma, CCT3 promotes proliferation through AKT signaling activation and ferroptosis inhibition 4. CCT3 overexpression is associated with poor prognosis in cervical cancer, lung cancer, and liver cancer 543. The protein serves as both a diagnostic biomarker and potential therapeutic target, with serum CCT3 showing superior diagnostic capacity compared to alpha fetoprotein in liver cancer 3.