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- W3048487796 abstract "Significance The PRL phosphatases are highly oncogenic when overexpressed. However, the mechanism by which they promote tumorigenesis is unknown. Here, we reveal PTEN as a putative PRL2 substrate and define a mechanism for PTEN degradation through PRL2-mediated PTEN dephosphorylation. These insights immediately place the PRL2 phosphatase into the PI3K/AKT pathway, one of the critical signaling networks altered in cancer. We further demonstrate in a preclinical model that removal of Prl2 in Pten +/− mice increases the level of PTEN and inhibits PTEN heterozygosity-induced tumorigenesis. Given the observed inverse correlation between PRL2 expression and PTEN level, targeting PRL2 serves as a potential PTEN restoration strategy to treat cancers caused by PTEN deficiency." @default.
- W3048487796 created "2020-08-18" @default.
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- W3048487796 date "2020-08-11" @default.
- W3048487796 modified "2023-10-16" @default.
- W3048487796 title "Mechanism of PRL2 phosphatase-mediated PTEN degradation and tumorigenesis" @default.
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- W3048487796 doi "https://doi.org/10.1073/pnas.2002964117" @default.
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