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Updated: May 29, 2025

Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase
Published on: February 12, 2019
Protein folding by the CCT/TRiC chaperone complex
Peter S Shen1, Barry M Willardson2
1Department of Biochemistry, School of Medicine, University of Utah, Salt Lake City UT 84112, USA.
Abstract:
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.
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