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Degradation of the ABA co-receptor ABI1 by PUB12/13 U-box E3 ligases
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Degradation of the ABA co-receptor ABI1 by PUB12/13 U-box E3 ligases
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Journal Article
Degradation of the ABA co-receptor ABI1 by PUB12/13 U-box E3 ligases
2015
Overview
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.
Signaling by the plant hormone abscisic acid (ABA) is regulated by the ABI1 protein phosphatase. Here Kong
et al.
propose that ABA signaling is fine-tuned by ubiquitination of ABI1 which promotes ABI degradation in response to ABA.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Pub. Group
Subject
/ 64
/ 82
/ 82/1
/ Arabidopsis Proteins - genetics
/ Arabidopsis Proteins - metabolism
/ Humanities and Social Sciences
/ Kinases
/ Mutants
/ Mutation
/ Phosphoprotein Phosphatases - genetics
/ Phosphoprotein Phosphatases - metabolism
/ Proteasome Endopeptidase Complex - metabolism
/ Proteins
/ Science
/ Seeds
