In the absence of Hh signaling, the majority of full-length GLI3 is partially processed by the proteasome to a shorter form that serves as the principal repressor of Hh target genes (Wang et al, 2000). Processing depends on phosphorylation at 6 sites by PKA, which primes the protein for subsequent phosphorylation at adjacent sites by CK1 and GSK3. The hyperphosphorylated protein is then a direct target for betaTrCP-dependent ubiquitination and proteasome-dependent processing (Wang and Li, 2006; Tempe et al, 2006; Wen et al, 2010; Schrader et al, 2011; Pan and Wang, 2007).
Tempe, D, Concordet, JP, Casas, M, Blanchet-Tournier, MF, Karaz, S
Pan, Y, Wang, B
Fallon, JF, Beachy, PA, Wang, B
Scales, SJ, Hongo, JA, Wen, X, Evangelista, M, Lai, CK, de Sauvage, FJ
Matouschek, A, Holmgren, RA, Schrader, EK, Harstad, KG
Wang, B, Li, Y
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