PKA phosphorylates GLI1

Stable Identifier
Reaction [transition]
Homo sapiens
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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
16705181 Multisite protein kinase A and glycogen synthase kinase 3beta phosphorylation leads to Gli3 ubiquitination by SCFbetaTrCP

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

Mol Cell Biol 2006
19056373 Phosphorylation of Gli2 by protein kinase A is required for Gli2 processing and degradation and the Sonic Hedgehog-regulated mouse development

Wang, C, Pan, Y, Wang, B

Dev. Biol. 2009
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, Oro, AE, Estay, IS, Jackson, PK, Zhen, H, Lokteva, LA

Genes Dev. 2006
Catalyst Activity

cAMP-dependent protein kinase activity of PKA catalytic subunit [ciliary base]

Inferred From
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