Protein folding by the CCT/TRiC chaperone complex

The chaperonin-containing TCP-1 (CCT) complex, also known as TRiC, is an abundant and essential molecular chaperone responsible for folding a significant portion of the eukaryotic proteome. Prominent CCT folding clients include cytoskeletal proteins such as actin and tubulin, and proteins with β-propeller folds. Recent advances in cryo-EM have provided unprecedented insights into CCT's substrate-specific folding mechanisms. This review summarizes these discoveries, emphasizing how CCT utilizes its unique structural features to recognize and fold diverse substrates.