Tubulin folding cofactor E-like protein (TBCEL)

Tubulin folding cofactor E-like protein (TBCEL) is a protein that regulates microtubule stability by binding alpha-tubulin and directly disrupting tubulin heterodimers[1][4]. Overexpression of TBCEL leads to microtubule depolymerization by promoting proteasomal degradation of free tubulin subunits, thus reducing the pool available for microtubule polymer formation[1]. Suppression of TBCEL increases stable microtubules and causes clustering of intracellular membranes around the microtubule-organizing center, indicating that TBCEL modulates tubulin turnover rather than dynamic microtubule behavior[1]. TBCEL’s activity is balanced by proteins like Op18/stathmin, which protect tubulin from TBCEL-induced degradation. In Drosophila, the homolog mulet (coding for TBCEL) is essential for the removal of cytoplasmic microtubules during spermatid individualization, further supporting its role in microtubule remodeling[2]. TBCEL is thought to function predominantly in the cytoskeleton and cytoplasm, and disease associations with gene alterations include specific types of leukoencephalopathy[4]. While it is a regulator of cytoskeletal structure, TBCEL is not currently considered a canonical therapeutic target, such as a receptor, enzyme, transporter, or ion channel[1][4].

Other names

Tubulin-specific chaperone cofactor E-like proteinLRRC35ElE-likecatastrophinleucine-rich repeat-containing protein 35tubulin-specific chaperone cofactor E-liketubulin-specific chaperone e-likeMGC10233mulet