Pka phosphorylates GLI1

Stable Identifier
R-NUL-5610740
Type
Reaction [transition]
Species
Mus musculus
Compartment
ReviewStatus
5/5
General
SVG |   | PPTX  | SBGN
Pka phosphorylates GLI1
Degradation of human GLI1 is abrogated in NIH 3T3 cells after treatment of cells with a PKA inhibitor, suggesting that like GLI2 and GLI3, GLI1 is a substrate for PKA-mediated phosphorylation. Consistent with this, GLI1 constructs lacking the PKA sites in the C-terminal do not bind beta TrCP and have enhanced protein stability relative to the wild type protein (Huntzicker et al, 2006).
Literature References
PubMed ID Title Journal Year
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
Participants
Catalyst Activity

protein serine/threonine kinase activity of PKA catalytic subunit [cytosol]

Orthologous Events
Authored
Reviewed
Created
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