The structural basis of eukaryotic chaperonin TRiC/CCT: Action and folding

• DOI: 10.1016/j.mocell.2024.100012
• Publication Date: 2024-01-26T16:44:56Z
• Authors: Hyunmin Kim; Junsun Park; Soung-Hun Roh
• Keywords: Chaperonin; Chaperone (clinical); Folding (DSP implementation); Co-chaperone; Adenosine triphosphate

Accurate folding of proteins in living cells often requires the cooperative support molecular chaperones. Eukaryotic group II chaperonin TRiC accomplishes this task by providing a chamber for substrate that is regulated an ATP hydrolysis-dependent cycle. Once delivered to and recognized TRiC, nascent enters undergoes release stepwise manner. During process, subunits cochaperones such as prefoldin (PFD) phosducin-like (PhLPs) interact with assist overall process substrate-specific Coevolution between components supposed consult binding specificity ultimately expand repertoire assisted chaperone network. This review describes guided network cooperation cochaperones, specifically focusing on recent progress structural analyses.