GLI1 is degraded by the proteasome after ubiquitination by ITCH

Stable Identifier
Reaction [omitted]
Homo sapiens
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In the absence of Hh signal, GLI1 is degraded by the proteasome. Degradation depends on GLI1 ubiquitination by SCF(beta-TrCP) and by the E3 ligase ITCH (Huntzicker et al, 2006; di Marcotullio et al, 2006, 2011).

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
17115028 Numb is a suppressor of Hedgehog signalling and targets Gli1 for Itch-dependent ubiquitination

De Smaele, E, Gulino, A, Sico, MA, Screpanti, I, Ferretti, E, Maroder, M, Alimandi, M, Di Marcotullio, L, Giannini, G, Po, A, Greco, A

Nat. Cell Biol. 2006
20818436 Numb activates the E3 ligase Itch to control Gli1 function through a novel degradation signal

Canettieri, G, Pietrosanti, L, MazzĂ , D, Screpanti, I, Greco, A, Coni, S, Gulino, A, De Smaele, E, Di Marcotullio, L, Infante, P, Ferretti, E, Moretti, M

Oncogene 2011
Catalyst Activity

endopeptidase activity of 26S proteasome [cytosol]

Orthologous Events
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