Research ArticleBiochemistry

A direct heterotypic interaction between the DIX domains of Dishevelled and Axin mediates signaling to β-catenin

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Science Signaling  10 Dec 2019:
Vol. 12, Issue 611, eaaw5505
DOI: 10.1126/scisignal.aaw5505

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DIX domains drive Wnt–β-catenin signaling

Dishevelled (Dvl) stimulates Wnt–β-catenin signaling by recruiting Axin, a component of the β-catenin destruction complex, to the Wnt signalosome, thus stabilizing β-catenin. Both Dvl-mediated activation and Axin-mediated repression of signaling require homopolymerization through the DIX domains of each protein. Through structural analysis and biochemical assays with the DIX domain of human Dvl and the DIX domain of human Axin (DAX), Yamanishi et al. found that the heterotypic interface between DIX and DAX resembled the interfaces observed in the individual homopolymers and that DIX-DAX heteropolymerization was favored over DAX-DAX homopolymerization. These findings support a model in which Dvl-Axin heterodimerization, mediated by DIX domains, drives the recruitment of Axin to the Wnt signalosome and disruption of the β-catenin destruction complex.

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