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Article

Structural basis for Ccd1 auto-inhibition in the Wnt pathway through homomerization of the DIX domain.

Scientific reports - 10 Aug 2017

Terawaki Shin-Ichi, Fujita Shohei, Katsutani Takuya, Shiomi Kensuke, Keino-Masu Kazuko, Masu Masayuki, Wakamatsu Kaori, Shibata Naoki, Higuchi Yoshiki

Abstract excerpt

Wnt signaling plays an important role in governing cell fate decisions. Coiled-coil-DIX1 (Ccd1), Dishevelled (Dvl), and Axin are signaling proteins that regulate the canonical pathway by controlling the stability of a key signal transducer β-catenin. These proteins contain the DIX domain with a ubiquitin-like fold, which mediates their interaction in the β-catenin destruction complex through dynamic head-to-tail...

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Identifiers

PMID: 28798413
DOI: 10.1038/s41598-017-08019-5
PMCID: PMC5552852

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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