1. Osmotic signaling releases PP2C-mediated inhibition of Arabidopsis SnRK2s via the receptor-like cytoplasmic kinase BIK1.
- Author
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Li, Guo-Jun, Chen, Kong, Sun, Shujing, and Zhao, Yang
- Abstract
Osmotic stress and abscisic acid (ABA) signaling are important for plant growth and abiotic stress resistance. Activation of osmotic and ABA signaling downstream of the PYL-type ABA receptors requires the release of SnRK2 protein kinases from the inhibition imposed by PP2Cs. PP2Cs are core negative regulators that constantly interact with and inhibit SnRK2s, but how osmotic signaling breaks the PP2C inhibition of SnRK2s remains unclear. Here, we report that an Arabidopsis receptor-like cytoplasmic kinase, BIK1, releases PP2C-mediated inhibition of SnRK2.6 via phosphorylation regulation. The dominant abi1-1 ABA-signaling mutation (G180D) disrupts PYL-PP2C interactions and disables PYL-initiated release of SnRK2s; in contrast, BIK1 releases abi1-1-mediated inhibition of SnRK2.6. BIK1 interacts with and phosphorylates SnRK2.6 at two tyrosine residues, which are critical for SnRK2.6 activation and function. Phosphorylation of the two tyrosine residues may affect the docking of the tryptophan "lock" of PP2C into SnRK2.6. Moreover, the bik1 mutant is defective in SnRK2 activation, stress-responsive gene expression, ABA accumulation, growth maintenance, and water loss under osmotic stress. Our findings uncover the critical role of BIK1 in releasing PP2C-mediated inhibition of SnRK2s under osmotic stress. Synopsis: Plants respond to a lack of water through a series of responses triggered by the hormone abscisic acid (ABA). This work shows that, under osmotic stress, SnRK2 and PP2C (components of the ABA signalling pathway) need to be activated by BIK1-mediated tyrosine phosphorylation of SnRK2s. BIK1 releases SnRK2.6 from PP2C binding and inhibition under osmotic stress. Release of SnRK2s from PP2Cs by BIK1 differs in mechanism from that of ABA and PYLs. Two tyrosine residues that are phosphorylated by BIK1 are critical for SnRK2.6-ABI1 interaction. The tryptophan lock of PP2C plays a critical role in PP2C-SnRK2.6 binding. BIK1 triggers early abscisic-acid-independent osmotic stress signals. [ABSTRACT FROM AUTHOR]
- Published
- 2024
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