Formation of tubulin folding intermediates by CCT/TriC

Stable Identifier
R-HSA-389960
Type
Pathway
Species
Homo sapiens
Compartment
cytosol
ReviewStatus
5/5
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Formation of tubulin folding intermediates by CCT/TriC
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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).
Literature References
PubMed ID Title Journal Year
8096061 Two cofactors and cytoplasmic chaperonin are required for the folding of alpha- and beta-tubulin

Cowan, NJ, Chow, RL, Gao, Y, Vainberg, IE

Mol Cell Biol 1993
11868281 Type II chaperonins, prefoldin, and the tubulin-specific chaperones

Lewis, SA, Cowan, NJ

Adv Protein Chem 2001
9265649 Tubulin subunits exist in an activated conformational state generated and maintained by protein cofactors

Rommelaere, H, Lewis, SA, Stearns, T, Cowan, NJ, Feierbach, B, Tian, G, Ampe, C

J Cell Biol 1997
1361170 Function in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits

Wall, JS, Nimmesgern, E, Hartl, FU, Tempst, P, Frydman, J, Erdjument-Bromage, H

EMBO J 1992
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Go Biological Process
protein folding (0006457)
Authored
Matthews, L  (2008-12-01)
Reviewed
Cowan, NJ  (2009-01-21)
Created
Matthews, L  (2009-01-22)
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