TBCC Human

The process of tubulin folding and dimerization is complex and requires the coordinated action of several cofactors, including TBCC. After the translation of α- and β-tubulin, these proteins are initially captured by chaperonins, which assist in their partial folding. However, the final folding and dimerization of tubulin require the involvement of specific cofactors, namely cofactors A, B, C, D, and E .

TBCC, in particular, is responsible for the final steps of this process. It interacts with other cofactors to form a super-complex that facilitates the release of correctly folded α/β-tubulin heterodimers. This release is catalyzed in the presence of GTP .

TBCC belongs to the TBCC family and plays a role in the regulation of centrosome and Golgi apparatus positioning, which has consequences on cell shape and migration . The protein consists of several domains, including a spectrin-like domain, which is crucial for its function .

The recombinant human TBCC protein is typically expressed in E. coli and purified using conventional chromatography techniques. It is often tagged with a His-tag at the N-terminus to facilitate purification .

Recombinant TBCC is widely used in research to study the mechanisms of tubulin folding and microtubule assembly. It is also used to investigate the role of microtubules in various cellular processes, including cell division, intracellular transport, and cell migration .