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<p>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 Ca<sup>2+</sup> signaling and Ca<sup>2+</sup>-dependent phosphorylation are essential for&#xa0;Al stress-responsive regulation of STOP1. Al exposure specifically induces rapid, spatio-temporally defined biphasic Ca<sup>2+</sup> signals in Arabidopsis roots and concomitantly activates the Ca<sup>2+</sup>-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 Ca<sup>2+</sup>-CPK28-STOP1 signaling axis critical for plant adaptation to Al stress.</p>

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CPK28-mediated Ca2+ signaling regulates STOP1 localization and accumulation to facilitate plant aluminum resistance

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2025年6月5日

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  • Yingtang Ma,
  • Hailiang Zheng,
  • Ina Schmitz-Thom,
  • Jiawen Wang,
  • Fanglin Zhou,
  • Chongyang Li,
  • Yaling Zhang,
  • Yiqiu Cheng,
  • Daisuke Miki,
  • Jörg Kudla,
  • Chao-Feng Huang

摘要

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.