The DIX domain of Dishevelled confers Wnt signaling by dynamic polymerization (Q41791636)

10 October 2017

The DIX domain of Dishevelled confers Wnt signaling by dynamic polymerization (English)

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Dishevelled segment polarity protein 2

10 October 2017

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GOA release 2020-03-11

author name string

Thomas Schwarz-Romond

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10 October 2017

Marc Fiedler

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10 October 2017

Naoki Shibata

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10 October 2017

P Jonathan G Butler

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10 October 2017

Akira Kikuchi

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10 October 2017

Yoshiki Higuchi

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10 October 2017

Mariann Bienz

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10 October 2017

27 May 2007

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Nature Structural & Molecular Biology

10 October 2017

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10 October 2017

14

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10 October 2017

484-492

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10 October 2017

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https://scigraph.springernature.com/pub.10.1038/nsmb1247

10 October 2017

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The Drosophila segment polarity gene dishevelled encodes a novel protein required for response to the wingless signal

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A frizzled homolog functions in a vertebrate Wnt signaling pathway

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Differential recruitment of Dishevelled provides signaling specificity in the planar cell polarity and Wingless signaling pathways

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Establishment of the dorsal-ventral axis in Xenopus embryos coincides with the dorsal enrichment of dishevelled that is dependent on cortical rotation

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The C-terminal cytoplasmic Lys-thr-X-X-X-Trp motif in frizzled receptors mediates Wnt/beta-catenin signalling

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Dishevelled phosphorylation, subcellular localization and multimerization regulate its role in early embryogenesis.

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Wnt signals across the plasma membrane to activate the beta-catenin pathway by forming oligomers containing its receptors, Frizzled and LRP.

31 March 2020

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Direct binding of the PDZ domain of Dishevelled to a conserved internal sequence in the C-terminal region of Frizzled

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DIX domains of Dvl and axin are necessary for protein interactions and their ability to regulate beta-catenin stability

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Interaction of axin and Dvl-2 proteins regulates Dvl-2-stimulated TCF-dependent transcription.

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Nuclear localization is required for Dishevelled function in Wnt/beta-catenin signaling

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The DIX domain targets dishevelled to actin stress fibres and vesicular membranes

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The Wnt signalling effector Dishevelled forms dynamic protein assemblies rather than stable associations with cytoplasmic vesicles.

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Dishevelled (Dvl-2) activates canonical Wnt signalling in the absence of cytoplasmic puncta.

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Identification of a domain of Axin that binds to the serine/threonine protein phosphatase 2A and a self-binding domain

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Axin contains three separable domains that confer intramolecular, homodimeric, and heterodimeric interactions involved in distinct functions

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Identifiers

DOI

10.1038/NSMB1247

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Dimensions Publication ID

10 October 2017

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