Tubulin-specific chaperone A is a protein that in humans is encoded by the TBCAgene.[1][2][3]
The product of this gene is one of four proteins (cofactors A, D, E, and C) involved in the pathway leading to correctly folded beta-tubulin from folding intermediates. Cofactors A and D are believed to play a role in capturing and stabilizing beta-tubulin intermediates in a quasi-native confirmation. Cofactor E binds to the cofactor D/beta-tubulin complex; interaction with cofactor C then causes the release of beta-tubulin polypeptides that are committed to the native state. This gene encodes chaperonin cofactor A.[3]
Guasch A, Aloria K, Pérez R, et al. (2002). "Three-dimensional structure of human tubulin chaperone cofactor A". J. Mol. Biol. 318 (4): 1139–49. doi:10.1016/S0022-2836(02)00185-7. PMID12054808.
Nolasco S, Bellido J, Gonçalves J, et al. (2005). "Tubulin cofactor A gene silencing in mammalian cells induces changes in microtubule cytoskeleton, cell cycle arrest and cell death". FEBS Lett. 579 (17): 3515–24. doi:10.1016/j.febslet.2005.05.022. PMID15963512.
Bruneel A, Labas V, Mailloux A, et al. (2006). "Proteomics of human umbilical vein endothelial cells applied to etoposide-induced apoptosis". Proteomics. 5 (15): 3876–84. doi:10.1002/pmic.200401239. PMID16130169.