PKA phosphorylates GLI3

Stable Identifier
Reaction [transition]
Homo sapiens
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Phosphorylation of GLI3 by PKA on up to six sites in the C-terminal region primes the protein for subsequent phosphorylation by CK1 and GSK3 and is required for the ubiquitin-mediated processing by the proteasome to yield the truncated repressor form (Tempe et al, 2006; Pan et al, 2006; Pan and Wang, 2007; Wang and Li, 2006). Processing of GLI3 is regulated in part by movement through the primary cilia, and disruption of intraflagellar transport abrogates processing (Wen et al, 2010)

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
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
20154143 Kinetics of hedgehog-dependent full-length Gli3 accumulation in primary cilia and subsequent degradation

Scales, SJ, Hongo, JA, Wen, X, Evangelista, M, Lai, CK, de Sauvage, FJ

Mol. Cell. Biol. 2010
16611981 Sonic hedgehog signaling regulates Gli2 transcriptional activity by suppressing its processing and degradation

Pan, Y, Bai, CB, Wang, B, Joyner, AL

Mol. Cell. Biol. 2006
16371461 Evidence for the direct involvement of {beta}TrCP in Gli3 protein processing

Wang, B, Li, Y

Proc. Natl. Acad. Sci. U.S.A. 2006
Catalyst Activity

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

Orthologous Events
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