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Clade A protein phosphatase 2Cs (PP2Cs) are abscisic acid (ABA) co-receptors that block ABA signalling by inhibiting the downstream protein kinases. ABA signalling is activated after PP2Cs are inhibited by ABA-bound PYR/PYL/RCAR ABA receptors (PYLs) in  Arabidopsis . However, whether these PP2Cs are regulated by other factors remains unknown. Here, we report that ABI1 (ABA-INSENSITIVE 1) can interact with the U-box E3 ligases PUB12 and PUB13, but is ubiquitinated only when it interacts with ABA receptors in an  in vitro  assay. A mutant form of ABI1-1 that is unable to interact with PYLs is more stable than the wild-type protein. Both ABI1 degradation and all tested ABA responses are reduced in  pub12 pub13  mutants compared with the wild type. Introducing the  abi1-3  loss-of-function mutation into  pub12 pub13  mutant recovers the ABA-insensitive phenotypes of the  pub12 pub13  mutant. We thus uncover an important regulatory mechanism for regulating ABI1 levels by PUB12 and PUB13.

Degradation of the ABA co-receptor ABI1 by PUB12/13 U-box E3 ligases