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

Stable Identifier
R-HSA-5610754
Type
Reaction [omitted]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
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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
16705181 Multisite protein kinase A and glycogen synthase kinase 3beta phosphorylation leads to Gli3 ubiquitination by SCFbetaTrCP

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

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

Fallon, JF, Beachy, PA, Wang, B

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

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

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
Participants
Participates
Catalyst Activity

endopeptidase activity of 26S proteasome [cytosol]

Orthologous Events
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