4.6 Review

Regulation of Dishevelled protein activity and stability by post-translational modifications and autophagy

期刊

TRENDS IN BIOCHEMICAL SCIENCES
卷 46, 期 12, 页码 1003-1016

出版社

CELL PRESS
DOI: 10.1016/j.tibs.2021.07.008

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资金

  1. National Key Research and Development Program of China [2017YFA0103601]
  2. National Natural Science Foundation of China [31988101, 31730056]

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Dishevelled (Dvl/Dsh) is a key component of Wnt signaling, essential for development processes in multicellular organisms. It acts as a branch-point of both beta-catenin-dependent canonical and beta-catenin-independent noncanonical pathways, dynamically interacting with multiple proteins to modulate Wnt signaling. The regulation of Dvl activity, localization, and stability by post-translational modifications, aggregation, and autophagy impacts its function in both Wnt signaling and biological processes.
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 beta-catenin-dependent canonical and beta-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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