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

doi:10.1016/j.redox.2020.101553

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

Pharmaceutical Sciences

Research output: Contribution to journal › Review article › peer-review

42 Scopus citations

Abstract

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 language	English
Article number	101553
Journal	Redox Biology
Volume	34
DOIs	https://doi.org/10.1016/j.redox.2020.101553
State	Published - Jul 2020

Bibliographical note

Funding Information:
The present study was supported by the grants (2018R1D1A1B06051438 and NRF-2015R1D1A1A01059571) from the National Research Foundation, Republic of Korea. Jiyoung Park was supported by the Health Fellowship Foundation.

Funding Information:
The present study was supported by the grants ( 2018R1D1A1B06051438 and NRF-2015R1D1A1A01059571 ) from the National Research Foundation, Republic of Korea . Jiyoung Park was supported by the Health Fellowship Foundation .

Publisher Copyright:
© 2020 The Authors

Keywords

PTEN
Peroxides
Prx dimerization
Prx hyperoxidation
Redox regulation
Trx dimerization

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10.1016/j.redox.2020.101553

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title = "Redox regulation of tumor suppressor PTEN in cell signaling",

abstract = "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.",

keywords = "PTEN, Peroxides, Prx dimerization, Prx hyperoxidation, Redox regulation, Trx dimerization",

author = "Ying Zhang and Jiyoung Park and Han, {Seong Jeong} and Yang, {Sung Yeul} and Yoon, {Hyun Joong} and Iha Park and Woo, {Hyun Ae} and Lee, {Seung Rock}",

note = "Funding Information: The present study was supported by the grants (2018R1D1A1B06051438 and NRF-2015R1D1A1A01059571) from the National Research Foundation, Republic of Korea. Jiyoung Park was supported by the Health Fellowship Foundation. Funding Information: The present study was supported by the grants ( 2018R1D1A1B06051438 and NRF-2015R1D1A1A01059571 ) from the National Research Foundation, Republic of Korea . Jiyoung Park was supported by the Health Fellowship Foundation . Publisher Copyright: {\textcopyright} 2020 The Authors",

year = "2020",

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doi = "10.1016/j.redox.2020.101553",

language = "English",

volume = "34",

journal = "Redox Biology",

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AU - Zhang, Ying

AU - Park, Jiyoung

AU - Han, Seong Jeong

AU - Yang, Sung Yeul

AU - Yoon, Hyun Joong

AU - Park, Iha

AU - Woo, Hyun Ae

AU - Lee, Seung Rock

N1 - Funding Information: The present study was supported by the grants (2018R1D1A1B06051438 and NRF-2015R1D1A1A01059571) from the National Research Foundation, Republic of Korea. Jiyoung Park was supported by the Health Fellowship Foundation. Funding Information: The present study was supported by the grants ( 2018R1D1A1B06051438 and NRF-2015R1D1A1A01059571 ) from the National Research Foundation, Republic of Korea . Jiyoung Park was supported by the Health Fellowship Foundation . Publisher Copyright: © 2020 The Authors

PY - 2020/7

Y1 - 2020/7

N2 - 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.

AB - 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.

KW - PTEN

KW - Peroxides

KW - Prx dimerization

KW - Prx hyperoxidation

KW - Redox regulation

KW - Trx dimerization

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DO - 10.1016/j.redox.2020.101553

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JO - Redox Biology

JF - Redox Biology

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Redox regulation of tumor suppressor PTEN in cell signaling

Abstract

Bibliographical note

Keywords

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