CKAP1/TBCB Protein, Human (His)

The CKAP1/TBCB protein exhibits a multifaceted role in the tubulin folding pathway, binding to alpha-tubulin folding intermediates subsequent to their interaction with cytosolic chaperonin, a pivotal step in the transition from newly synthesized tubulin to properly folded heterodimer. It plays a crucial role in regulating tubulin heterodimer dissociation and may function as a negative regulator of axonal growth. The formation of a supercomplex composed of cofactors A to E is integral to its mechanism. Cofactors A and D function by capturing and stabilizing tubulin in a quasi-native conformation, while cofactor E binds to the cofactor D-tubulin complex. The subsequent interaction with cofactor C leads to the release of tubulin polypeptides committed to the native state. Additionally, cofactors B and E can form a heterodimer that binds to alpha-tubulin, enhancing their capacity to dissociate tubulin heterodimers. CKAP1/TBCB also interacts with GAN and DCTN1, further expanding its functional associations in cellular processes.