Heat shock protein 70 (HSP70) is a chaperone that facilitates protein folding and transport, with essential roles in maintaining cell homeostasis and survival. In addition to its chaperone function in proteostasis, HSP70 can act as a signaling molecule. Gungor, Vanharanta, et al. studied the effects of rHSP70 on human primary monocyte-derived macrophage foam cells that accumulate cholesterol, which leads to artherosclerosis. They found that HSP70 exerts atheroprotective effects and that this can be mechanistically explained by HSP70 mediated stimulation of the liver X receptor, the master regulator of cholesterol removal.