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
Affiliations
Ying Zhang
Department of Biochemistry, Department of Biomedical Sciences, Research Center for Aging and Geriatrics, Research Institute of Medical Sciences, Chonnam National University Medical School, Gwangju, 501-190, Republic of Korea
Jiyoung Park
College of Pharmacy, Graduate School of Pharmaceutical Sciences, Ewha Womans University, Seoul, 120-750, Republic of Korea
Seong-Jeong Han
COTDE Inc. 19-3, Ugakgol-gil, Susin-myeon, Cheonan-si, Chungcheongnam-do, 330-882, Republic of Korea
Sung Yeul Yang
Department of Biochemistry, Department of Biomedical Sciences, Research Center for Aging and Geriatrics, Research Institute of Medical Sciences, Chonnam National University Medical School, Gwangju, 501-190, Republic of Korea
Hyun Joong Yoon
Department of Biochemistry, Department of Biomedical Sciences, Research Center for Aging and Geriatrics, Research Institute of Medical Sciences, Chonnam National University Medical School, Gwangju, 501-190, Republic of Korea
Iha Park
Department of Biochemistry, Department of Biomedical Sciences, Research Center for Aging and Geriatrics, Research Institute of Medical Sciences, Chonnam National University Medical School, Gwangju, 501-190, Republic of Korea
Hyun Ae Woo
College of Pharmacy, Graduate School of Pharmaceutical Sciences, Ewha Womans University, Seoul, 120-750, Republic of Korea
Seung-Rock Lee
Department of Biochemistry, Department of Biomedical Sciences, Research Center for Aging and Geriatrics, Research Institute of Medical Sciences, Chonnam National University Medical School, Gwangju, 501-190, Republic of Korea; Corresponding author.
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.
