Although direct phosphorylation of GLI1 by PKA has not been demonstrated, deletion of the putative PKA sites abrogates the interaction of GLI1 with beta-TrCP and stabilizes GLI1 protein levels; similarly, treatment of GLI1-expressing cells with PKA inhibitors delays the kinetics of GLI1 degradation (Huntzicker et al, 2006). These data are consistent with a role for PKA-mediated phosphorylation in promoting the proteasome-dependent degradation of GLI1 in the absence of Hh signal, as is the case for GLI2 and GLI3 (Huntzicker et al, 2006; Tempe et al, 2006; Pan and Wang, 2007; Pan et al, 2009). Potential roles for CK2 and GSK3 in promoting the phosphorylation-dependent degradation of GLI1 have not been investigated.
Tempe, D, Concordet, JP, Casas, M, Blanchet-Tournier, MF, Karaz, S
Wang, C, Pan, Y, Wang, B
Pan, Y, Wang, B
Huntzicker, EG, Oro, AE, Estay, IS, Jackson, PK, Zhen, H, Lokteva, LA
cAMP-dependent protein kinase activity of PKA catalytic subunit [ciliary base]
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