Expression and Post-translational Modification of Heat Shock Protein 27 (HSP27) in Cancer

Abstract

Heat shock protein 27 (HSP27) is induced by heat shock, environmental, and pathophysiological stressors. HSP27 functions as a molecular chaperone and an anti-apoptotic protein in cells. Dynamic changes such as phosphorylation and oligomerization of HSP27 allow cells to adapt to changes in physiological functions and mount a protective response to damage. HSP27 is highly expressed in aggressive cancers, where it is involved in numerous pro-tumorigenic signaling pathways and is associated with poor prognosis and treatment resistant. This review focuses on the recent findings of the role of HSP27, particularly posttranslational modification of HSP27 in cancer, and the strategies for therapeutic purposes by using HSP27 inhibitors.