After phosphorylation and ubiquitination, GLI3 is processed by the proteasome to an 83-kDa repressor form that lacks the C-terminal activation domain (Wang et al, 2000; Tempe et al, 2006; Wang and Li, 2006). Partial processing appears to rely on at least three features of the GLI3 protein: the folded N-terminal zinc finger domain, an adjacent simple linker sequence, and the degron in the C-terminus that contains the phosphorylation and ubiquitination target residues (Pan and Wang, 2007; Schrader et al, 2011). The C-terminal end of the processed repressor form is not precisely defined.