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Related Experiment Video

Updated: Jan 7, 2026

Tyramide Signal Amplification for the Immunofluorescent Staining of ZBP1-Dependent Phosphorylation of RIPK3 and MLKL After HSV-1 Infection in Human Cells

Tyramide Signal Amplification for the Immunofluorescent Staining of ZBP1-Dependent Phosphorylation of RIPK3 and MLKL After HSV-1 Infection in Human Cells

Published on: October 20, 2022

PRICKLE3 protects VANGL proteins from CK1-mediated phosphorylation and RNF43-mediated degradation.

Katarzyna A Radaszkiewicz¹, Tomasz W Radaszkiewicz¹, Pavla Kolářová¹

¹Department of Experimental Biology, Faculty of Science, Masaryk University, Brno, Czechia.

Communications Biology

|December 27, 2025

Summary

This summary is machine-generated.

PRICKLE3 is a key regulator of WNT/planar cell polarity (PCP) signaling. It stabilizes VANGL1/2 proteins by preventing phosphorylation, crucial for cell polarity and tissue development.

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Published on: July 29, 2014

Area of Science:

Cell Biology
Developmental Biology
Molecular Biology

Background:

The WNT/planar cell polarity (PCP) pathway is vital for vertebrate development, controlling cell polarity and tissue organization.
Individual PRICKLE protein functions within the WNT/PCP pathway are not fully elucidated.
Understanding PRICKLE protein mechanisms is crucial for comprehending developmental processes and diseases.

Purpose of the Study:

To identify and characterize the role of PRICKLE3 in WNT/PCP signaling.
To elucidate the molecular mechanisms by which PRICKLE3 regulates WNT/PCP components.
To provide novel molecular tools for studying the PRICKLE protein family.

Main Methods:

Enhanced proximity biotinylation (miniTurboID) coupled with mass spectrometry to identify protein interactions.
Immunoblotting and live imaging to assess protein stability and localization.
Functional assays in human cells, Xenopus laevis, and zebrafish (Danio rerio) embryos.

Main Results:

PRICKLE3 was identified as a central regulator of WNT/PCP signaling across species.
PRICKLE3 associates with VANGL1 and VANGL2 at the plasma membrane.
PRICKLE3 selectively stabilizes VANGL1/2 by inhibiting Casein kinase 1ε (CK1ε)-mediated phosphorylation and modulating RNF43 activity.
PRICKLE1 did not exhibit similar stabilizing effects on VANGL proteins.

Conclusions:

PRICKLE3 employs a unique mechanism to stabilize VANGL complexes by inhibiting CK1ε and suppressing RNF43.
This PRICKLE3-specific function is critical for WNT/PCP pathway regulation, impacting cell polarity and tissue architecture.
The study provides a detailed interactome and valuable tools for future research on PRICKLE proteins in development and disease.