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.
Highlights
FERONIA (FER) is a versatile receptor-like kinase (RLK) that controls most aspects of plant cellular activity [1,2]
We show that rapid alkalinization factor 1 (RALF1)-FER signaling increases the abundance of ErbB3-binding protein 1 (EBP1) protein, which accumulates in the nucleus and controls gene expression
EBP1 protein binds to the promoters of some RALF1-FER-regulated
Summary
FERONIA (FER) is a versatile receptor-like kinase (RLK) that controls most aspects of plant cellular activity [1,2]. Our recent work has shown that two FER-like receptor (FLR) genes in rice are crucial for cell growth [11]. The roles of FER in stress response might be attributable to its function in regulating abscisic acid (ABA) and rapid alkalinization factors (RALFs) signal transduction [12,16,17]. Studies have shown that fer mutants show a hypersensitive response to exogenous ABA with respect to stomatal closure and primary root growth [17]. Previous studies have shown that mutations in FER can alter fungal invasion [21,22], implicating FER in immune responses Along this line, other RALF-family peptides—including RALF17, RALF23, and RALF33—may work with FER to regulate 22 amino acid fragment of bacterial flagellin (flg22)-triggered reactive oxygen species (ROS) burst [16]. FER works with several other proteins, such as RPM1-induced protein kinase (RIPK) [23] and LLG1 [24], to transmit RALF1 signal
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