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Updated: Oct 23, 2025

Assays for the Degradation of Misfolded Proteins in Cells
Published on: August 28, 2016
Regulation of Dishevelled protein activity and stability by post-translational modifications and autophagy
1The State Key Laboratory of Membrane Biology, Tsinghua-Peking Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing, 100084, China.
Abstract:
As a key component of Wnt signaling, Dishevelled (Dvl/Dsh) plays essential roles in development processes and adult tissue homeostasis in multicellular organisms, and its deregulation results in human development disorders and other diseases. Dvl integrates and relays complex Wnt signals by acting as a branch-point of β-catenin-dependent canonical and β-catenin-independent noncanonical pathways. It dynamically interacts with multiple proteins to modulate Wnt signaling, while its activity and stability are tightly controlled by other proteins. This Review summarizes the current understanding of regulation of Dvl activity, localization, and stability by post-translational modifications, aggregation, and autophagy, and the impacts on Dvl function in both Wnt signaling and biological processes.
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