CPK28-mediated Ca2+ signaling regulates STOP1 localization and accumulation to facilitate plant aluminum resistance
Yingtang Ma,
Hailiang Zheng,
Ina Schmitz-Thom,
Jiawen Wang,
Fanglin Zhou,
Chongyang Li,
Yaling Zhang,
Yiqiu Cheng,
Daisuke Miki,
Jörg Kudla and
Chao-Feng Huang ()
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Yingtang Ma: Chinese Academy of Sciences
Hailiang Zheng: Chinese Academy of Sciences
Ina Schmitz-Thom: Universität Münster
Jiawen Wang: Chinese Academy of Sciences
Fanglin Zhou: Chinese Academy of Sciences
Chongyang Li: Chinese Academy of Sciences
Yaling Zhang: Chinese Academy of Sciences
Yiqiu Cheng: Chinese Academy of Sciences
Daisuke Miki: Chinese Academy of Sciences
Jörg Kudla: Universität Münster
Chao-Feng Huang: Chinese Academy of Sciences
Nature Communications, 2025, vol. 16, issue 1, 1-18
Abstract:
Abstract The transcription factor SENSITIVE TO PROTON RHIZOTOXICITY 1 (STOP1) functions as a crucial integrator of plant responses to various stresses, including aluminum (Al) stress. Its stability and accumulation are modulated by stress-specific post-translational mechanisms such as phosphorylation and ubiquitination. However, the upstream signaling mechanisms governing these modifications remain poorly understood. Here, we reveal that Ca2+ signaling and Ca2+-dependent phosphorylation are essential for Al stress-responsive regulation of STOP1. Al exposure specifically induces rapid, spatio-temporally defined biphasic Ca2+ signals in Arabidopsis roots and concomitantly activates the Ca2+-dependent kinase CPK28. Al-activated CPK28 phosphorylates STOP1 at Ser163, a modification that promotes the nuclear localization of STOP1 and prevents its degradation by inhibiting its interaction with the F-box protein RAE1. This phosphorylation enhances STOP1 accumulation and Al resistance. Our findings identify Ser163 phosphorylation as a key molecular switch and establish a Ca2+-CPK28-STOP1 signaling axis critical for plant adaptation to Al stress.
Date: 2025
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-60427-8
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DOI: 10.1038/s41467-025-60427-8
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