Heat shock protein 27: Structure, function, cellular role and inhibitors

Abstract

Hsp27 is an important heat shock protein found in all organisms from prokaryotes to mammals. It is a structurally conserved ATP-independent protein, present in both normal and abnormal tissues. Its expression and induction occur under stressed conditions. The self-association to form oligomers and subsequent equilibrium between oligomer and dimer play critical roles in regulating Hsp27’s function. Site-specific phosphorylation of Hsp27 regulates this equilibrium, controlling the activity of Hsp27. Hsp27’s molecular chaperone activity includes interacting with a large number of proteins and regulating their folding states. Significant levels of Hsp27 expression have been observed in many diseases, including cancer, neuronal diseases and cardiac diseases. Herein we describe the current understanding of Hsp27’s structure, function, cellular role and inhibitors.