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A role of Dishevelled in relocating Axin to the plasma membrane during wingless signaling. | LitMetric

A role of Dishevelled in relocating Axin to the plasma membrane during wingless signaling.

Curr Biol

MRC Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 2QH, United Kingdom.

Published: May 2003

AI Article Synopsis

  • Wnt signaling is crucial for regulating gene transcription during normal and cancerous cell development, with beta-catenin as a key player in this pathway.
  • In the absence of Wnt signals, beta-catenin is targeted for degradation by a complex involving Axin and various kinases, including CKI and GSK3, while the APC tumor suppressor also aids in its degradation.
  • The study shows that Wingless signaling causes Axin to move from the cytoplasm to the plasma membrane, a process dependent on the protein Dishevelled (Dsh), which may help to inhibit beta-catenin degradation.

Article Abstract

Wnt signaling causes changes in gene transcription that are pivotal for normal and malignant development. A key effector of the canonical Wnt pathway is beta-catenin, or Drosophila Armadillo. In the absence of Wnt ligand, beta-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 beta-catenin substrate and kinases (casein kinase I [CKI] and glycogen synthase kinase 3 beta [GSK3]). The Adenomatous polyposis coli (APC) tumor suppressor also binds to the Axin complex, thereby promoting the degradation of beta-catenin. In Wnt signaling, this complex is inhibited; as a consequence, beta-catenin accumulates and binds to TCF proteins to stimulate the transcription of Wnt target genes. Wnt-induced inhibition of the Axin complex depends on Dishevelled (Dsh), a cytoplasmic protein that can bind to Axin, 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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Source
http://dx.doi.org/10.1016/s0960-9822(03)00370-1DOI Listing

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