Regulation of heat shock proteins 70 and their role in plant immunity

Heat shock proteins 70 (HSP70s) are steadily gaining more attention in the field of plant biotic interactions. Though their regulation and activity in plants are much less well characterized than are those of their counterparts in mammals, accumulating evidence indicates that the role of HSP70-mediated defense mechanisms in plant cells is indispensable. In this review, we summarize current knowledge of HSP70 post-translational control in plants. We comment on the phytohormonal regulation of HSP70 expression and protein abundance, and identify a prominent role for cytokinin in HSP70 control. We outline HSP70s' subcellular localizations, chaperone activity, and chaperone-mediated protein degradation. We focus on the role of HSP70s in plant pathogen-associated molecular pattern-triggered immunity and effector-triggered immunity, and discuss the contribution of different HSP70 subfamilies to plant defense against pathogens. The extensive regulation of HSP70 has received little attention in plant science. Here, we summarize current knowledge gained in large-scale profiling experiments and highlight HSP70s' role in plant immunity.

Automated summary

This article provides a summary of HSP70 post-translational control in plants, including the regulation of HSP70 expression and protein abundance by plant hormones, subcellular localization of HSP70s, chaperone activity, and their involvement in plant immunity against pathogens. The extensive regulation of HSP70 in plants has received little attention, and this review highlights the importance of HSP70 in plant defense mechanisms.