Current Biology
Volume 13, Issue 11, 27 May 2003, Pages 960-966
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A Role of Dishevelled in Relocating Axin to the Plasma Membrane during Wingless Signaling

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Abstract

Wnt signaling causes changes in gene transcription that are pivotal for normal and malignant development 1, 2. A key effector of the canonical Wnt pathway is β-catenin, or Drosophila Armadillo. In the absence of Wnt ligand, β-catenin is phosphorylated by the Axin complex, which earmarks it for rapid degradation by the ubiquitin system. Axin acts as a scaffold in this complex, to assemble β-catenin substrate and kinases (casein kinase I [CKI] and glycogen synthase kinase 3β [GSK3]) 3, 4. The Adenomatous polyposis coli (APC) tumor suppressor also binds to the Axin complex, thereby promoting the degradation of β-catenin 5, 6. In Wnt signaling, this complex is inhibited; as a consequence, β-catenin accumulates and binds to TCF proteins to stimulate the transcription of Wnt target genes 1, 2. Wnt-induced inhibition of the Axin complex depends on Dishevelled (Dsh) 7, 8, 9, a cytoplasmic protein that can bind to Axin 10, 11, but the mechanism of this inhibition is not understood. Here, we show that Wingless signaling causes a striking relocation of Drosophila Axin from the cytoplasm to the plasma membrane. This relocation depends on Dsh. It may permit the subsequent inactivation of the Axin complex by Wingless signaling.

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