TriC/CCT forms a binary complex with unfolded alpha- or beta-tubulin (Frydman et al., 1992; Gao et al., 1993). The tubulin folding intermediates produced by TriC are unstable (Gao et al., 1993). Five additional protein cofactors (cofactor A-E) are required for the generation of properly folded alpha- and beta-tubulin and for the formation of alpha/beta-tubulin heterodimers (Gao et al., 1993) (Tian et al., 1997, Cowan and Lewis 2001).
|1361170||Function in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits||EMBO J||1992|
|9265649||Tubulin subunits exist in an activated conformational state generated and maintained by protein cofactors||J Cell Biol||1997|
|8096061||Two cofactors and cytoplasmic chaperonin are required for the folding of alpha- and beta-tubulin||Mol Cell Biol||1993|
|11868281||Type II chaperonins, prefoldin, and the tubulin-specific chaperones||Adv Protein Chem||2001|