Tubulin-folding cofactor D (TBCD)

Tubulin-folding cofactor D is a chaperone protein involved in the cytosolic folding and assembly of β-tubulin, which is required to build functional microtubules, a key component of the cytoskeleton[1][2][3][4]. TBCD captures and stabilizes β-tubulin intermediates in a near-native state, enabling their proper incorporation into α/β-tubulin heterodimers, with further action by cofactors C and E[1][2][4]. TBCD also functions as a centrosomal protein, necessary for the recruitment of the γ-tubulin ring complex at the centrosome and microtubule nucleation[2][3]. Mutations in the TBCD gene cause rare, often severe, neurodevelopmental and neurodegenerative disorders, characterized by microcephaly, developmental delay, epilepsy, and hypotonia[2]. TBCD forms a regulatory complex with ARL2 and β-tubulin, crucial for microtubule assembly in neural and other cell types[2]. There are currently no direct drug interactions or established targeted therapies for TBCD, and it is not widely considered a classic therapeutic target, such as a receptor or enzyme[1][2][4].

Other names

Tubulin-specific chaperone DCofactor D