Trans-kingdom coupling of redox signaling to environmental cell stress responses through multiphase partitioning
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Reactive Oxygen Species (ROS) signaling is a conserved biological process with parallel functions in all evolutionary branches of life. Using a cysteine proteomics screen, we identified an ancient protein, Receptor for Activated C Kinase 1 (RACK1) as a redox-regulated mediator of signaling to multiple environmental stimuli. RACK1 regulates a generalized stress response through specific oxidation of a conserved cysteine. Following induction of diverse stressors, RACK1 partitions to cytosolic redox-privileged, condensates. These condensates provide a compartmentalized platform for cellular ROS signaling, regulating ribosomal function and protein translation, and function in the human host response to bacterial infection. We find that oxidized RACK1 condensates are conserved through evolution with analogous stress response behavior in bacteria and yeast indicating a ubiquitous and ancient stress sensor-effector system.
