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Stress-induced activation of receptor signaling by protease-mediated cleavage
Author(s) -
Sen Hou,
Jie Zhang,
Ping He
Publication year - 2021
Publication title -
biochemical journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.706
H-Index - 265
eISSN - 1470-8728
pISSN - 0264-6021
DOI - 10.1042/bcj20200941
Subject(s) - proteases , protease , cleavage (geology) , receptor , microbiology and biotechnology , intracellular , signal transduction , protease activated receptor , protein precursor , proteolysis , biology , biochemistry , chemistry , enzyme , immunology , paleontology , thrombin , platelet , fracture (geology)
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.

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