Deubiquitination of dishevelled by usp14 is required for wnt signaling

H. Jung, B. G. Kim, W. H. Han, J. H. Lee, J. Y. Cho, W. S. Park, M. M. Maurice, J. K. Han, M. J. Lee, D. Finley, E. H. Jho

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92 Scopus citations


Dishevelled (Dvl) is a key regulator of Wnt signaling both in the canonical and non-canonical pathways. Here we report the identification of a regulatory domain of ubiquitination (RDU) in the C-terminus of Dvl. Mutations in the RDU resulted in accumulation of polyubiquitinated forms of Dvl, which were mainly K63 linked. Small interfering RNA-based screening identified Usp14 as a mediator of Dvl deubiquitination. Genetic and chemical suppression of Usp14 activity caused an increase in Dvl polyubiquitination and significantly impaired downstream Wnt signaling. These data suggest that Usp14 functions as a positive regulator of the Wnt signaling pathway. Consistently, tissue microarray analysis of colon cancer revealed a strong correlation between the levels of Usp14 and β-catenin, which suggests an oncogenic role for Usp14 via enhancement of Wnt/β-catenin signaling.

Original languageEnglish
Article numbere64
StatePublished - 2013


  • Usp14
  • Wnt
  • deubiquitinase
  • dishevelled
  • ubiquitination


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