Galangin Suppresses the Proliferation of β-Catenin Response Transcription-Positive Cancer Cells by Promoting Adenomatous Polyposis Coli/Axin/Glycogen Synthase Kinase-3β-Independent β-Catenin Degradation

2011 ◽  
Vol 79 (6) ◽  
pp. 1014-1022 ◽  
Author(s):  
Jungsug Gwak ◽  
Jingyo Oh ◽  
Munju Cho ◽  
Soo Kyung Bae ◽  
Im-Sook Song ◽  
...  
PLoS ONE ◽  
2020 ◽  
Vol 15 (10) ◽  
pp. e0240746
Author(s):  
Lauren E. King ◽  
Hui-Hua Zhang ◽  
Cathryn M. Gould ◽  
Daniel W. Thomas ◽  
Lachlan W. Whitehead ◽  
...  

Human Cell ◽  
2014 ◽  
Vol 27 (2) ◽  
pp. 78-84 ◽  
Author(s):  
Sandra Regina Lepri ◽  
Leonardo Campos Zanelatto ◽  
Patrícia Benites Gonçalves da Silva ◽  
Daniele Sartori ◽  
Lucia Regina Ribeiro ◽  
...  

2000 ◽  
Vol 20 (6) ◽  
pp. 2228-2238 ◽  
Author(s):  
Keiji Itoh ◽  
Alena Antipova ◽  
Marianne J. Ratcliffe ◽  
Sergei Sokol

ABSTRACT Signaling by the Wnt family of secreted proteins plays an important role in animal development and is often misregulated in carcinogenesis. Wnt signal transduction is controlled by the rate of degradation of β-catenin by a complex of proteins including glycogen synthase kinase 3 (GSK3), adenomatous polyposis coli, and Axin. Dishevelled is required for Wnt signal transduction, and its activation results in stabilization of β-catenin. However, the biochemical events underlying this process remain largely unclear. Here we show thatXenopus Dishevelled (Xdsh) interacts with aXenopus Axin-related protein (XARP). This interaction depends on the presence of the Dishevelled-Axin (DIX) domains in both XARP and Xdsh. Moreover, the same domains are essential for signal transduction through Xdsh. Finally, our data point to a possible mechanism for signal transduction, in which Xdsh prevents β-catenin degradation by displacing GSK3 from its complex with XARP.


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