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

ABSTRACT: The Wnt-β-catenin signaling pathway regulates embryonic development and tissue homeostasis throughout the animal kingdom. Signaling through this pathway crucially depends on the opposing activities of two cytoplasmic multiprotein complexes: the Axin destruction complex, which destabilizes the downstream effector β-catenin, and the Dishevelled signalosome, which inactivates the Axin complex and thus enables β-catenin to accumulate and operate a transcriptional switch in the nucleus. These complexes are assembled by dynamic head-to-tail polymerization of the DIX domains of Axin or Dishevelled, respectively, which increases their avidity for signaling effectors. Axin also binds to Dishevelled through its DIX domain. Here, we report the crystal structure of the heterodimeric complex between th

SUBMITTER: Yamanishi K 

PROVIDER: S-EPMC6923138 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature