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. 2020 Aug 15;17(3):707–725. doi: 10.20892/j.issn.2095-3941.2020.0056

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Copyright: © 2020, Cancer Biology & Medicine

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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SHP2-deficiency-mediated dephosphorylation and activation of GSK3β through inhibition of the PI3K/AKT signaling pathway. (A) SHP2 knockout decreased the protein levels of phosphorylated AKT (T308) and phosphorylated ERK (T202/Y204) in 2 breast cancer cell lines. (B) Western blot analysis of the levels of Cyclin D1, total and phosphorylated GSK3β (Ser9), and total and phosphorylated ERK (T202/Y204) in 2 breast cancer cell lines pretreated with different concentrations of PD98059 for 6 h. (C) Inhibition of the PI3K/AKT pathway with LY294002 decreased the expression of phosphorylated GSK3β (Ser9) in 2 breast cancer cell lines. The cells were pretreated with different concentrations of LY294002 for 6 h, lysed, and analyzed via western blot.