Rheostatic Control of ABA Signaling through HOS15-Mediated OST1 Degradation

• Published in: Molecular plant 2019-11, Vol.12 (11), p.1447-1462
• Main Authors: Ali, Akhtar, Kim, Jae Kyoung, Jan, Masood, Khan, Haris Ali, Khan, Irfan Ullah, Shen, Mingzhe, Park, Junghoon, Lim, Chae Jin, Hussain, Shah, Baek, Dongwon, Wang, Kai, Chung, Woo Sik, Rubio, Vicente, Lee, Sang Yeol, Gong, Zhizhong, Kim, Woe Yeon, Bressan, Ray A., Pardo, Jose M., Yun, Dae-Jin
• Format: Article
• Language: English
• Subjects: ABA signaling; ABI1/2; Abscisic Acid - metabolism; Arabidopsis - cytology; Arabidopsis - genetics; Arabidopsis - metabolism; Arabidopsis Proteins - genetics; Arabidopsis Proteins - metabolism; Chromosomal Proteins, Non-Histone - metabolism; drought stress; Droughts; Gene Expression Regulation, Plant; HOS15; Models, Biological; Mutation; OST1; Proteasome Endopeptidase Complex - metabolism; protein degradation and stability; Protein Kinases - genetics; Protein Kinases - metabolism; Proteolysis; Signal Transduction; Stress, Physiological
• ISSN: 1674-2052; 1752-9867
• DOI: 10.1016/j.molp.2019.08.005

Dehydrating stresses trigger the accumulation of abscisic acid (ABA), a key plant stress-signaling hormone that activates Snf1-Related Kinases (SnRK2s) to mount adaptive responses. However, the regulatory circuits that terminate the SnRK2s signal relay after acclimation or post-stress conditions remain to be defined. Here, we show that the desensitization of the ABA signal is achieved by the regulation of OST1 (SnRK2.6) protein stability via the E3-ubiquitin ligase HOS15. Upon ABA signal, HOS15-induced degradation of OST1 is inhibited and stabilized OST1 promotes the stress response. When the ABA signal terminates, protein phosphatases ABI1/2 promote rapid degradation of OST1 via HOS15. Notably, we found that even in the presence of ABA, OST1 levels are also depleted within hours of ABA signal onset. The unexpected dynamics of OST1 abundance are then resolved by systematic mathematical modeling, demonstrating a desensitizing feedback loop by which OST1-induced upregulation of ABI1/2 leads to the degradation of OST1. This model illustrates the complex rheostat dynamics underlying the ABA-induced stress response and desensitization. This work demonstrates that HOS15 negatively regulates ABA signaling by interacting with and affecting OST1 protein stability, which leads to controlled turnover of ABA signaling and drought-stress response.