Table of Contents
Cancers, Volume 11, Issue 4 (April 2019)
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Cover Story (view full-size image) With this work, we provide mechanistic evidence that ANXA2, via its reactive Cys-8 residue, binds [...] Read more. With this work, we provide mechanistic evidence that ANXA2, via its reactive Cys-8 residue, binds to PTEN and that co-expression of PTEN and ANXA2 inhibits AKT phosphorylation on Ser473. These data together with our observation that ANXA2 depleted cells show enhanced phosphorylation of AKT following either EGF/EGFR activation or RasV12 transformation compared to controls support that direct regulation of PTEN by ANXA2 might constitute an important mechanism in regulating AKT following H2O2-dependent signaling. Furthermore, we reveal that ANXA2 inversely regulates the expression of the peroxidase, PRDX2, in a ROS-dependent manner. The activation of the EGF/PI3K/AKT or RAS/PI3K/AKT networks enables Rac to bind to and activate NOX. This drives the increase in intracellular H2O2 and induces PRDX2 to compensate for the REDOX unbalance in ANXA2 depleted cells. View this paper