Degradation of the ABA Co-receptor ABI1 by PUB12/13 U-box E3 Ligases

Overview

Journal Nat Commun

Specialty Biology

Date 2015 Oct 21

PMID 26482222

Citations 129

Authors

Lingyao Kong

Jinkui Cheng

Yujuan Zhu

Yanglin Ding

Jingjing Meng

Zhizhong Chen

Qi Xie

Yan Guo

Jigang Li

Shuhua Yang

Zhizhong Gong

Affiliations

Soon will be listed here.

Abstract

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.

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