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).
Pan, Y, Wang, B
Tempe, D, Casas, M, Karaz, S, Blanchet-Tournier, MF, Concordet, JP
Wang, B, Fallon, JF, Beachy, PA
Wen, X, Lai, CK, Evangelista, M, Hongo, JA, de Sauvage, FJ, Scales, SJ
Schrader, EK, Harstad, KG, Holmgren, RA, Matouschek, A
Wang, B, Li, Y
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