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Identification of EPP1 shows its essential role in mediating signal between activated SYMRK receptor and cytoplasmic components.
Legume symbiosis with nitrogen-fixing bacteria is controlled by a cascade of signaling events leading to root nodule development. While plant cell-surface receptors initiate this process, the link between receptors and cytoplasmic signaling components remains unclear. Here we identify Early Phosphorylated Protein 1 (EPP1) as a central mediator of this pathway. EPP1 is recruited to the activated SYMRK receptor, where it is phosphorylated on a key serine residue, an event essential and sufficient to propagate symbiotic signaling. We provide structural and functional validation of the SYMRK-EPP1 signaling complex and demonstrate that EPP1 is required for root nodule formation. Synthetic engineering of the SYMRK-EPP1 interaction bypasses the need for symbiotic bacteria to initiate the pathway and triggers nodule organogenesis. These findings establish EPP1 as a crucial cytoplasmic component between receptor activation and intracellular signaling, advancing our understanding of nitrogen-fixing symbiosis.
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Noergaard et al. (2025) studied this question.
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