PP2A inactivation by ROS accumulation

Abstract

In this issue of Blood, Low and colleagues show that reactive oxygen species (ROS)-mediated phosphorylation of Bcl-2 overcomes chemoresistance in hematopoietic malignancies and other cancers and that this function is mediated by selective nitration of Y289 on the Bcl-2-bound B56d subunit of protein phosphatase 2A (PP2A), which interferes with the interaction of Bcl-2 with the PP2A catalytic core, leading to increased Bcl-2 S70 phosphorylation.