Redox regulation of tumor suppressor PTEN in cell signaling
- 주제(키워드) Peroxides , Prx dimerization , Prx hyperoxidation , PTEN , Redox regulation , Trx dimerization
- 등재 SCIE, SCOPUS
- OA유형 Green Published, gold
- 발행기관 Elsevier B.V.
- 발행년도 2020
- 총서유형 Journal
- URI http://www.dcollection.net/handler/ewha/000000168921
- 본문언어 영어
- Published As https://dx.doi.org/10.1016/j.redox.2020.101553
- PubMed https://pubmed.ncbi.nlm.nih.gov/32413744
- 저작권 이화여자대학교 논문은 저작권에 의해 보호받습니다.
초록/요약
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. © 2020 The Authors
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