Tubulin-specific chaperone C

Tubulin-specific chaperone C (TBCC) is a 346-amino acid protein that functions as a tubulin-folding protein, catalyzing the final step of the tubulin folding pathway (UniProt: Q15814). This molecular chaperone is essential for proper assembly and maturation of α/β-tubulin dimers, which form the structural backbone of microtubules.

TBCC is involved in cytoskeletal organization and is broadly expressed in tissues requiring dynamic microtubule dynamics. No disease associations are documented in UniProt for this protein, though tubulin folding defects may impact cellular processes dependent on stable microtubule networks.

In Alzheimer's Disease, TBCC shows significant downregulation in post-mortem AD brain tissue relative to age-matched controls, with a mean log2 fold-change of −0.95 across subcellular fractions (Chaparral AD proteomics). This reduction was detected by quantitative proteomics (TMT-labeled DDA) in human AD brain and may reflect diminished capacity for tubulin maintenance in AD neurons, potentially contributing to cytoskeletal dysfunction observed in the disease.