Stress-induced activation of receptor signaling by protease-mediated cleavage

Biochem J. 2021 May 28;478(10):1847-1852. doi: 10.1042/BCJ20200941.

Abstract

Plants encode a large number of proteases in activating intracellular signaling through proteolytic cleavages of various protein substrates. One type of the substrates is proligands, including peptide hormones, which are perceived by cell surface-resident receptors. The peptide hormones are usually first synthesized as propeptides, and then cleaved by specific proteases for activation. Accumulating evidence indicates that the protease-mediated cleavage of proligands can be triggered by environmental stresses and subsequently activates plant stress signaling. In this perspective, we highlight several recent publications and provide an update about stress-induced cleavage of propeptides and receptor-associated components by proteases in the activation of cell surface-resident receptor signaling in plants. We also discuss some questions and future challenges in the research of protease functions in plant stress response.

Keywords: peptide hormone; plant immunity; protease; receptor kinase.

MeSH terms

  • Peptide Hydrolases / metabolism*
  • Plant Proteins / metabolism*
  • Plants / metabolism*
  • Proteolysis
  • Receptors, Cell Surface / metabolism*
  • Stress, Physiological*

Substances

  • Plant Proteins
  • Receptors, Cell Surface
  • Peptide Hydrolases