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Cited by 316

The DOI matches its Crossref record; 55 of the 55 references it cites were found in a registry or an index.

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

Open access
Kong, Lingyao, Cheng, Jinkui, Zhu, Yujuan, Ding, Yanglin, Meng, Jingjing, Chen, Zhizhong, Xie, Qi, Guo, Yan, Li, Jigang, Yang, Shuhua, Gong, Zhizhong·2015·Nature Communications

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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Crossref · 10.1038/ncomms9630

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Metadata

Authors
Kong, L., Cheng, J., Zhu, Y., Ding, Y., Meng, J., Chen, Z., Xie, Q., Guo, Y., Li, J., Yang, S., & Gong, Z.
Venue
Nature Communications
Published
2015-10-20
Volume
6
Issue
1
Pages
8630-8630
ISSN
2041-1723 (ISSN-L)
OpenAlex
W2254998690
Cited by
316
References
55
FWCI
22.60
Type
journal article
Language
en
Open access
gold

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