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- Title
EBP1 nuclear accumulation negatively feeds back on FERONIA-mediated RALF1 signaling.
- Authors
Li, Chiyu; Liu, Xuanming; Qiang, Xiaonan; Li, Xiaoyan; Li, Xiushan; Zhu, Sirui; Wang, Long; Wang, Yuan; Liao, Hongdong; Luan, Sheng; Yu, Feng
- Abstract
FERONIA (FER), a plasma membrane receptor-like kinase, is a central regulator of cell growth that integrates environmental and endogenous signals. A peptide ligand rapid alkalinization factor 1 (RALF1) binds to FER and triggers a series of downstream events, including inhibition of Arabidopsis H+-ATPase 2 activity at the cell surface and regulation of gene expression in the nucleus. We report here that, upon RALF1 binding, FER first promotes ErbB3-binding protein 1 (EBP1) mRNA translation and then interacts with and phosphorylates the EBP1 protein, leading to EBP1 accumulation in the nucleus. There, EBP1 associates with the promoters of previously identified RALF1-regulated genes, such as CML38, and regulates gene transcription in response to RALF1 signaling. EBP1 appears to inhibit the RALF1 peptide response, thus forming a transcription–translation feedback loop (TTFL) similar to that found in circadian rhythm control. The plant RALF1-FER-EBP1 axis is reminiscent of animal epidermal growth factor receptor (EGFR) signaling, in which EGF peptide induces EGFR to interact with and phosphorylate EBP1, promoting EBP1 nuclear accumulation to control cell growth. Thus, we suggest that in response to peptide signals, plant FER and animal EGFR use the conserved key regulator EBP1 to control cell growth in the nucleus. Author summary: Receptor-like kinase FERONIA (FER) is an important regulator of plant growth and stress response and is activated by binding its peptide ligand, rapid alkalinization factor 1 (RALF1). However, how FER, a plasma membrane–localized receptor protein, regulates gene expression in the nucleus remains unclear. Here, we show that RALF1-FER signaling increases the abundance of ErbB3-binding protein 1 (EBP1) protein, which then accumulates in the nucleus and controls gene expression. The receptor kinase FER also directly interacts with and phosphorylates EBP1, a required step for EBP1 accumulation in the nucleus. Ultimately, EBP1 protein binds to the promoters of some RALF1-FER-regulated genes and inhibits their expression, leading to a negative regulation of RALF1-FER response. This study thus reveals a link between a plasma membrane receptor and the control of gene expression in the nucleus and establishes a similar mode of action for EBP1 in both animals and plants.
- Subjects
EPIDERMAL growth factor receptors; GENETIC regulation; PEPTIDES; PROTEIN binding; PLANT regulators
- Publication
PLoS Biology, 2018, Vol 16, Issue 10, p1
- ISSN
1544-9173
- Publication type
Article
- DOI
10.1371/journal.pbio.2006340