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Figure 2


Fig. 2. Effect of pharmacological or genetic inactivation of class IA PI3K isoforms on the activation of small GTPases and PTEN. (A,B) Equal volumes of cell lysates of the indicated BMMs were subjected to pull-down assay with GTP-PBD, followed by detection of precipitated Rac1 by western blotting. Total cell lysates were resolved and immunoblotted for Rac1. Graphs represent the mean ± s.e.m. of three experiments. *P<0.05; **P<0.01 when compared with cells treated with vehicle only for each time point or with WT cells. (C,D) Equal volumes of cell lysates of the indicated BMMs were subjected to pull-down assay with GST-RBD, followed by western blot detection of precipitated RhoA. Total cell lysates were resolved on the same SDS-PAGE gel and immunoblotted for RhoA. Graphs for BMMs represent the mean ± s.e.m. of three experiments. *P<0.05; **P<0.01, compared with cells treated with vehicle only for each time point or with WT cells. (E) BMMs were pre-treated for 1 h with PW12 (0.5 µM), TGX155 (0.5 µM) or IC87114 (5 µM), followed by assay of PTEN lipid phosphatase activity as described (left panel). One representative experiment done in triplicate is shown (*P<0.05). Right panels show the effect of genetic inactivation of p110{delta} or p110{alpha} on PTEN lipid phosphatase activity. PTEN was immunoprecipitated from the respective BMM lysates followed by determination of its phosphatase activity towards synthetic PIP3 by ELISA (Echelon). One representative experiment done in triplicate is shown (*P<0.05).





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