Enhanced redox factor 1 (REF1)-modulated p53 stabilization and JNK1 dissociation in response to selenomethionine

Hwa Jin Jung, Hye Lim Kim, Young Rok Seo

Research output: Contribution to journalArticlepeer-review

2 Scopus citations


Aim: p53 is reportedly activated without any genotoxicity through redox modulation of redox factor 1 (REF1). REF1 is documented to modulate the redox status under selenomethionine (SeMet). In this study, we investigated the mechanism of p53 stabilization by SeMet. Materials and Methods: We mainly used ubiquitination assay and immunoprecipitation to determine the potential role of REF1 and c-jun N-terminal kinase 1 (JNK) in modulation of p53 stabilization by SeMet. Results: The amount of ubiquitinated p53 decreased significantly under SeMet treatment, suggesting that SeMet might inhibit the proteasome-dependent degradation of p53. In addition, we observed that JNK was considerably associated with p53 in REF1 siRNA-treated cells, implying a possible role for SeMet-induced REF1 activity in modulation of the interaction between JNK and p53 via changes in p53 redox status. Conclusion: Our results suggest that the alternate mechanism of p53 stabilization by SeMet might provide an important clue in elucidating the molecular mechanism of chemopreventative compounds against various oxidative stresses.

Original languageEnglish (US)
Pages (from-to)3645-3652
Number of pages8
JournalAnticancer Research
Issue number9
StatePublished - Sep 1 2013


  • Cancer prevention
  • JNK
  • P53
  • Protein stability
  • Redox factor 1
  • Selenomethionine
  • Ubiquitination

ASJC Scopus subject areas

  • Oncology
  • Cancer Research


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