The protein phosphatase OsPP1a dephosphorylates and stabilizes CatC to scavenge excess H2O2 and enhance salt tolerance in rice
Yan Wang, YuTing Yi, ZeLin Xu, Ye Tian, DeMing Mao, ZhenDie Luo, ZhengKun Zhou, Sheng-Nan Hu, YanNing Tan, XinHui Zhao, Lei Yang, DongYing Tang, YuanZhu Yang, WenBang Tang, Cong Liu, XuanMing Liu, Ji
Journal:Plant Communications
IF:13.7
DOI:10.1016/j.xplc.2026.101824
PMID:41846314
Published:2026-03-16
research field:分子生物学植物生物学胁迫生理学遗传学生物化学
Abstract
Catalase (CAT) plays a central role in maintaining H 2 O 2 homeostasis during stress response, yet how phosphatase-mediated dephosphorylation modulates CAT activity and stability remains unclear. Here, we identified a protein phosphatase OsPP1a as a positive regulator of salt tolerance in rice ( Oryza sativa L.). OsPP1a directly dephosphorylates CatC at Thr-292 in the peroxisome, thereby enhancing its stability and enzymatic activity by inhibiting E3 ubiquitin ligase APIP6-mediated ubiquitination and degradation. Consistently, OsPP1a -overexpressing lines exhibit enhanced salt and oxidative tolerance with a lower phospho-threonine level of CATs. Phosphatase activity and seminal root growth assays further indicate that OsPP1a acts as a critical regulator balancing salt tolerance and growth in rice. Importantly, OsPP1a overexpression markedly mitigates salt-induced grain yield loss. Together, these results shed light on the mechanisms of CAT switch-on and stabilization by phosphatases and provide a strategy for breeding highly salt-tolerant rice.
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