PKA phosphorylates GLI1

Stable Identifier
Homo sapiens
Locations in the PathwayBrowser

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.

Literature References
PubMed ID Title Journal Year
19056373 Phosphorylation of Gli2 by protein kinase A is required for Gli2 processing and degradation and the Sonic Hedgehog-regulated mouse development

Pan, Y, Wang, C, Wang, B

Dev. Biol. 2009
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
16421275 Dual degradation signals control Gli protein stability and tumor formation

Huntzicker, EG, Estay, IS, Zhen, H, Lokteva, LA, Jackson, PK, Oro, AE

Genes Dev. 2006
Participant Of
Catalyst Activity
Catalyst Activity
cAMP-dependent protein kinase activity of PKA catalytic subunit [ciliary base]
Physical Entity
Inferred From