Redox regulation of tumor suppressor PTEN in cell signaling

Ying Zhang, Jiyoung Park, Seong Jeong Han, Sung Yeul Yang, Hyun Joong Yoon, Iha Park, Hyun Ae Woo, Seung Rock Lee

Research output: Contribution to journalReview articlepeer-review

53 Scopus citations


Phosphatase and tensin homologs deleted on chromosome 10 (PTEN) is a potent tumor suppressor and often dysregulated in cancers. Cellular PTEN activity is restrained by the oxidation of active-site cysteine by reactive oxygen species (ROS). Recovery of its enzymatic activity predominantly depends on the availability of cellular thioredoxin (Trx) and peroxiredoxins (Prx), both are important players in cell signaling. Trx and Prx undergo redox-dependent conformational changes through the oxidation of cysteine residues at their active sites. Their dynamics are essential for protein functionality and regulation. In this review, we summarized the recent advances regarding the redox regulation of PTEN, with a specific focus on our current state-of-the-art understanding of the redox regulation of PTEN. We also proposed a tight association of the redox regulation of PTEN with Trx dimerization and Prx hyperoxidation, providing guidance for the identification of novel therapeutic targets.

Original languageEnglish
Article number101553
JournalRedox Biology
StatePublished - Jul 2020

Bibliographical note

Publisher Copyright:
© 2020 The Authors


  • PTEN
  • Peroxides
  • Prx dimerization
  • Prx hyperoxidation
  • Redox regulation
  • Trx dimerization


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