6VCC

Cryo-EM structure of the Dvl2 DIX filament

6VCC の概要

• エントリーDOI: 10.2210/pdb6vcc/pdb
• EMDBエントリー: 21148
• 分子名称: Segment polarity protein dishevelled homolog DVL-2 (1 entity in total)
• 機能のキーワード: dishevelled, dix domain, wnt signaling, signaling protein
• 由来する生物種: Mus musculus (Mouse)
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 112002.56

構造登録者

Enos, M.,Kan, W.,Muennich, S.,Chen, D.H.,Skiniotis, G.,Weis, W.I. (登録日: 2019-12-20, 公開日: 2020-04-29, 最終更新日: 2024-03-06)

主引用文献

Kan, W.,Enos, M.D.,Korkmazhan, E.,Muennich, S.,Chen, D.H.,Gammons, M.V.,Vasishtha, M.,Bienz, M.,Dunn, A.R.,Skiniotis, G.,Weis, W.I.
Limited Dishevelled/Axin oligomerization determines efficiency of Wnt/ beta-catenin signal transduction.
Elife, 9:-, 2020

PubMed Abstract: In Wnt/β-catenin signaling, the transcriptional coactivator β-catenin is regulated by its phosphorylation in a complex that includes the scaffold protein Axin and associated kinases. Wnt binding to its coreceptors activates the cytosolic effector Dishevelled (Dvl), leading to the recruitment of Axin and the inhibition of β-catenin phosphorylation. This process requires interaction of homologous DIX domains present in Dvl and Axin, but is mechanistically undefined. We show that Dvl DIX forms antiparallel, double-stranded oligomers in vitro, and that Dvl in cells forms oligomers typically <10 molecules at endogenous expression levels. Axin DIX (DAX) forms small single-stranded oligomers, but its self-association is stronger than that of DIX. DAX caps the ends of DIX oligomers, such that a DIX oligomer has at most four DAX binding sites. The relative affinities and stoichiometry of the DIX-DAX interaction provide a mechanism for efficient inhibition of β-catenin phosphorylation upon Axin recruitment to the Wnt receptor complex.

PubMed: 32297861
DOI: 10.7554/eLife.55015

実験手法

ELECTRON MICROSCOPY (3.6 Å)