Tubulin-specific chaperone E (TBCE) (TBCE)

Tubulin-specific chaperone E (TBCE) is a critical protein involved in the folding and dimerization of alpha- and beta-tubulin, which are essential for microtubule formation and stability (UniProt Q15813). TBCE acts as one of five tubulin-specific chaperones (A-E) that capture and fold tubulin monomers into functional heterodimers (PubMed: 10436023). Mutations in the TBCE gene lead to a deficiency in functional protein, resulting in impaired microtubule assembly and severe developmental disorders, most notably Sanjad-Sakati syndrome (SSS) and Kenny-Caffey syndrome type 1 (KCS1) (OMIM: 604933). These conditions are characterized by permanent hypoparathyroidism, extreme growth failure, and distinct dysmorphic features (NCBI Gene: 6905). While there are currently no approved pharmacological agents that directly target TBCE mRNA or protein, the mRNA is a potential candidate for replacement therapies aimed at restoring chaperone function in affected patients. Research in this area focuses on using mRNA-based delivery systems or gene therapy to mitigate the cytoskeletal defects and endocrine deficiencies associated with TBCE loss-of-function. Overexpression or dysregulation of TBCE has also been implicated in certain cancers, suggesting its role in maintaining the microtubule network is vital for cellular proliferation (PubMed: 26451371).

Other names

Tubulin folding cofactor ECofactor EHRDKCS1Sanjad-Sakati syndrome protein

Restoration of functional protein levels via mRNA replacement or gene therapy to facilitate tubulin heterodimer assembly.