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March 5, 2026PLANT PHYSIOLOGY3 citations

Decoding pollen hydration: the role of FERONIA-mediated signaling in stigmatic actin cytoskeleton dynamics

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YHYongjun HeSXShuo XuXLXin-qin Liu

Key Points

  • The aim is to uncover the molecular mechanisms of FERONIA-mediated signaling in pollen hydration and actin cytoskeleton dynamics.
  • Investigated actin organization in stigmatic papillae of Arabidopsis lacking FERONIA
  • Analyzed interaction between RALF33 and actin depolymerizing factor ADF3
  • Compared pollen hydration rates between wild type and ADF3 mutant plants
  • Examined phosphorylation of ADF3 by FERONIA in response to RALF33
  • Absence of FERONIA disrupted actin cytoskeleton organization in stigmatic papillae
  • RALF33 counteracted actin depolymerization induced by Latrunculin B
  • ADF3 mutant showed slower pollen hydration compared to wild type
  • FERONIA phosphorylated ADF3 at specific residues, impacting actin disassembly

Abstract

During pollination, the dry stigma exhibits high selectivity in facilitating the hydration of pollen. Pollen Coat B-class peptides (PCP-Bs) compete with stigmatic rapid alkalinization factor peptides RALF23/33 for interaction with stigmatic receptor kinase FERONIA (FER)/ANJEA (ANJ) to promote pollen hydration. However, the molecular mechanisms underlying the FER-mediated signaling pathway involved in pollen hydration remain largely unexplored. Here, we discovered that the absence of FER in Arabidopsis (Arabidopsis thaliana) leads to alteration of actin cytoskeleton organization in stigmatic papillae and that RALF33 effectively counteracts the stigmatic actin depolymerization induced by Latrunculin B treatment. We next identified that ADF3, an actin depolymerizing factor, interacts with the cytoplasmic domain of FER. The mutant of ADF3 supported a significantly slower rate of pollen hydration compared to the wild type. Moreover, FER phosphorylated ADF3 at Thr52 and Thr94 residues in response to RALF33, repressing its actin disassembly activity and stabilizing actin organization in stigmatic papillae. Interestingly, Pollen Coat B-class peptide PCP-Bγ induced stigmatic actin remodeling via ADF3, potentially via FER, thereby facilitating pollen hydration. Taken together, this study reveals that FER-mediated signaling modulates actin cytoskeleton organization within stigmatic papillae by regulating ADF3 activity, thereby controlling stigma accessibility for pollen hydration.

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Cite This Study

He et al. (2026) studied this question.

synapsesocial.com/papers/69a91de0d6127c7a504c1269https://doi.org/10.1093/plphys/kiag117
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