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Reviews citing this publication (1)
- The structural basis of eukaryotic chaperonin TRiC/CCT: Action and folding. Kim H, Park J, Roh SH. Mol Cells 47 100012 (2024)
Structural basis of plp2-mediated cytoskeletal protein folding by TRiC/CCT.
Abstract
The cytoskeletal proteins tubulin and actin are the obligate substrates of TCP-1 ring complex/Chaperonin containing TCP-1 (TRiC/CCT), and their folding involves co-chaperone. Through cryo-electron microscopy analysis, we present a more complete picture of TRiC-assisted tubulin/actin folding along TRiC adenosine triphosphatase cycle, under the coordination of co-chaperone plp2. In the open S1/S2 states, plp2 and tubulin/actin engaged within opposite TRiC chambers. Notably, we captured an unprecedented TRiC-plp2-tubulin complex in the closed S3 state, engaged with a folded full-length