Glypicans shield the Wnt lipid moiety to enable signalling at a distance.

Nature
Ian J McGoughJean-Paul Vincent

Abstract

A relatively small number of proteins have been suggested to act as morphogens-signalling molecules that spread within tissues to organize tissue repair and the specification of cell fate during development. Among them are Wnt proteins, which carry a palmitoleate moiety that is essential for signalling activity1-3. How a hydrophobic lipoprotein can spread in the aqueous extracellular space is unknown. Several mechanisms, such as those involving lipoprotein particles, exosomes or a specific chaperone, have been proposed to overcome this so-called Wnt solubility problem4-6. Here we provide evidence against these models and show that the Wnt lipid is shielded by the core domain of a subclass of glypicans defined by the Dally-like protein (Dlp). Structural analysis shows that, in the presence of palmitoleoylated peptides, these glypicans change conformation to create a hydrophobic space. Thus, glypicans of the Dlp family protect the lipid of Wnt proteins from the aqueous environment and serve as a reservoir from which Wnt proteins can be handed over to signalling receptors.

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Citations

Aug 1, 2020·Nature Reviews. Molecular Cell Biology·Paulina Strzyz
Sep 30, 2020·Journal of Cell Science·Tamás MatusekPascal P Thérond
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Methods Mentioned

BETA
biolayer interferometry
biosensors
size exclusion chromatography
glycosylation
transgenic
PCR
Immunoprecipitation
immunoprecipitations
Assay
transfection

Software Mentioned

PYMOL
ImageJ
SigmaPlot
GRADE webserver
INKSCAPE
refine
DIALS
Photoshop
AIMLESS
phenix

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