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

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

Stable Identifier

R-HSA-5610754

Type

Reaction [omitted]

Species

Homo sapiens

Compartment

cytosol

ReviewStatus

5/5

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

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