GLI3 is partially degraded by the proteasome to yield the GLI3 repressor

Stable Identifier
Reaction [omitted]
Homo sapiens
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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.

Literature References
PubMed ID Title Journal Year
17283082 A novel protein-processing domain in Gli2 and Gli3 differentially blocks complete protein degradation by the proteasome

Pan, Y, Wang, B

J. Biol. Chem. 2007
16705181 Multisite protein kinase A and glycogen synthase kinase 3beta phosphorylation leads to Gli3 ubiquitination by SCFbetaTrCP

Tempe, D, Casas, M, Karaz, S, Blanchet-Tournier, MF, Concordet, JP

Mol Cell Biol 2006
10693759 Hedgehog-regulated processing of Gli3 produces an anterior/posterior repressor gradient in the developing vertebrate limb

Wang, B, Fallon, JF, Beachy, PA

Cell 2000
21921029 A three-part signal governs differential processing of Gli1 and Gli3 proteins by the proteasome

Schrader, EK, Harstad, KG, Holmgren, RA, Matouschek, A

J. Biol. Chem. 2011
16371461 Evidence for the direct involvement of {beta}TrCP in Gli3 protein processing

Wang, B, Li, Y

Proc. Natl. Acad. Sci. U.S.A. 2006
Catalyst Activity

endopeptidase activity of 26S proteasome [cytosol]

Orthologous Events
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