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