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Jiang, Hao; Tang, Buyun; Xie, Zhouli; Nolan, Trevor; Ye, Huaxun; Song, Gao‐Yuan; Walley, Justin; Yin, Yanhai
The Plant journal : for cell and molecular biology, December 2019, 2019-12-00, 20191201, Volume: 100, Issue: 5Journal Article
Plant steroid hormones brassinosteroids (BRs) regulate plant growth and development at many different levels. Recent research has revealed that stress‐responsive NAC (petunia NAM and Arabidopsis ATAF1, ATAF2, and CUC2) transcription factor RD26 is regulated by BR signaling and antagonizes BES1 in the interaction between growth and drought stress signaling. However, the upstream signaling transduction components that activate RD26 during drought are still unknown. Here, we demonstrate that the function of RD26 is modulated by GSK3‐like kinase BIN2 and protein phosphatase 2C ABI1. We show that ABI1, a negative regulator in abscisic acid (ABA) signaling, dephosphorylates and destabilizes BIN2 to inhibit BIN2 kinase activity. RD26 protein is stabilized by ABA and dehydration in a BIN2‐dependent manner. BIN2 directly interacts and phosphorylates RD26 in vitro and in vivo. BIN2 phosphorylation of RD26 is required for RD26 transcriptional activation on drought‐responsive genes. RD26 overexpression suppressed the brassinazole (BRZ) insensitivity of BIN2 triple mutant bin2 bil1 bil2, and BIN2 function is required for the drought tolerance of RD26 overexpression plants. Taken together, our data suggest a drought signaling mechanism in which drought stress relieves ABI1 inhibition of BIN2, allowing BIN2 activation. Sequentially, BIN2 phosphorylates and stabilizes RD26 to promote drought stress response. Significance Statement RD26 is a key regulator of dehydration and drought tolerance in plants, however the post‐transcriptional regulation of RD26 is largely unknown. In this study, we found that BIN2, a GSK3‐like kinase, integrates upstream signaling of growth and drought stress to modulate RD26 through phosphorylation. Our findings provide a potential target to manipulate drought tolerance by engineering RD26 phosphorylation sites in crops and other commercially significant plants.
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