Heat Shock Proteins (Hsps) Mediated Signalling Pathways During Abiotic Stress Conditions

Abstract The perception of abiotic stress and signal transduction to switch on adaptive innate responses are crucial steps in plant persistence under adverse environmental conditions. The ability of plants to respond to different stresses by maintaining protein in functional active form is of high importance and essential for cell survival. This is possible with the functional activity of heat shock proteins (Hsps), which play a role in maintaining the cellular homeostasis, and preserving the nonnative protein in a competent state for further remodeling as well as in signal transduction. Hsps mediate the stress signals either directly or indirectly, and play an important role in maintaining the homeostasis of plant cells under adverse stress conditions. Much research has been conducted to understand the complex mechanisms of the Hsps including Hsp70/90, ATPase-coupled conformational modifications, and interactions with cochaperones. In addition to this, several signaling proteins including MAP kinases, Ca 2+ regulated proteins, Hsfs, reactive oxygen species are seen to be interacting with Hsps. In this study, we discuss the signal transduction of different Hsps, and their role in different signaling mechanisms.