Pja2 inhibits Wnt/β-catenin signaling by reducing the level of TCF/LEF1

Yonghee Song, Somyung Lee, Jeong Rae Kim, Eek Hoon Jho

Research output: Contribution to journalArticlepeer-review

11 Scopus citations


Ubiquitination of proteins plays an essential role in various cellular processes, including protein degradation, DNA repair, and cell signaling pathways. Previous studies have shown that protein ubiquitination is implicated in regulating pluripotency as well as fate determination of stem cells. To identify how protein ubiquitination affects differentiation of embryonic stem cells, we analyzed microarray data, which are available in the public domain, of E3 ligases and deubiquitinases whose levels changed during stem cell differentiation. Expression of pja2, a member of the RING-type E3 ligase family, was up-regulated during differentiation of stem cells. Wnt/β-catenin signaling is one of the most important signaling pathways for regulation of the self-renewal and differentiation of embryonic stem cells. Pja2 was shown to bind to TCF/LEF1, which are transcriptional factors for Wnt/β-catenin signaling, and regulate protein levels by ubiquitination, leading to down-regulation of Wnt signaling activity. Based on these results, we suggest that E3 ligase Pja2 regulates stem cell differentiation by controlling the level of TCF/LEF1 by ubiquitination.

Original languageEnglish
Pages (from-to)242-247
Number of pages6
JournalInternational Journal of Stem Cells
Issue number2
StatePublished - 1 Nov 2018


  • Differentiation
  • E3 ligase
  • Embryonic stem cell
  • Pja2
  • TCF/LEF1
  • Wnt


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