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Updated: Jul 4, 2026

Phosphoproteomic Strategy for Profiling Osmotic Stress Signaling in Arabidopsis
Published on: June 25, 2020
OsMAPK6 Phosphorylates and Degrades OsCATA to Regulate H2O2 Homeostasis Conferring Resistance to Bacterial Blight in
Lihan Wang1, Jie Chen1, Guixin Yuan2
1National Key Laboratory of Crop Genetic Improvement, Hubei Hongshan Laboratory, Huazhong Agricultural University, Wuhan, China.
Abstract:
Mitogen-activated protein kinase (MAPK) cascades have been extensively reported to be involved in biotic and abiotic stress processes by regulating hydrogen peroxide (H2O2) homeostasis in plants. However, the detailed mechanisms by which MAPK cascades regulate H2O2 homeostasis in response to bacterial pathogens in rice remain largely unknown. Here, we demonstrate that rice CATALASE A (OsCATA) is a new substrate of OsMAPK6 and negatively regulates rice resistance to Xanthomonas oryzae pv. oryzae (Xoo) by directly suppressing H2O2 accumulation. Our results showed that OsMAPK6 interacts with OsCATA and specifically phosphorylates it at serine 460. The phosphorylation of OsCATA by OsMAPK6 attenuates OsCATA accumulation and reduces its catalase activity in vitro. The OsMAPK6-overexpressing (OsMAPK6-OE) plants showed lower catalase activity and higher accumulation of H2O2 compared with wild-type plants. The oscata mutant plants generated by the clustered regularly interspaced short palindromic repeats (CRISPR)/CRISPR-associated protein 9 (Cas9) strategy showed higher accumulation of H2O2 and increased resistance to Xoo. Together, these results suggest that the OsMAPK6-OsCATA module is involved in modulating rice H2O2 homeostasis and immunity.
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