Protein phosphatase 2A modulation and connection with miRNAs and natural products

Protein phosphatase 2A (PP2A), a heterotrimeric holoenzyme (scaffolding, catalytic, and regulatory subunits), regulates dephosphorylation for more than half of serine/threonine phosphosites and exhibits diverse cellular functions. Although several studies on natural products and miRNAs have emphasiz...

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Published inEnvironmental toxicology Vol. 39; no. 6; pp. 3612 - 3627
Main Authors Chuang, Ya‐Ting, Yen, Ching‐Yu, Tang, Jen‐Yang, Chang, Fang‐Rong, Tsai, Yi‐Hong, Wu, Kuo‐Chuan, Chien, Tsu‐Ming, Chang, Hsueh‐Wei
Format Journal Article
LanguageEnglish
Published Hoboken, USA John Wiley & Sons, Inc 01.06.2024
Wiley Subscription Services, Inc
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Summary:Protein phosphatase 2A (PP2A), a heterotrimeric holoenzyme (scaffolding, catalytic, and regulatory subunits), regulates dephosphorylation for more than half of serine/threonine phosphosites and exhibits diverse cellular functions. Although several studies on natural products and miRNAs have emphasized their impacts on PP2A regulation, their connections lack systemic organization. Moreover, only part of the PP2A family has been investigated. This review focuses on the PP2A‐modulating effects of natural products and miRNAs' interactions with potential PP2A targets in cancer and non‐cancer cells. PP2A‐modulating natural products and miRNAs were retrieved through a literature search. Utilizing the miRDB database, potential PP2A targets of these PP2A‐modulating miRNAs for the whole set (17 members) of the PP2A family were retrieved. Finally, PP2A‐modulating natural products and miRNAs were linked via a literature search. This review provides systemic directions for assessing natural products and miRNAs relating to the PP2A‐modulating functions in cancer and disease treatments.
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ISSN:1520-4081
1522-7278
1522-7278
DOI:10.1002/tox.24199