Work

The cleaved C-terminal domain of GmERS1-1 modulates cell cycle via GmACR1

Year: 2026

Type: preprint

Abstract: SUMMARY Ethylene signaling orchestrates plant development and stress adaptation, yet how post-translational modifications of its receptors coordinate growth regulation remains unresolved. Here, we uncover a proteolytic processing mechanism of the soybean ethylene receptor GmERS1-1 that directly gates cell cycle progression. The GmERS1-1 mutants exhibit elevated yield under field conditions, whereas overexpression suppresses growth and hypersensitizes plants to ethylene. Ethylene triggers nuclear translocation of C-terminal domain (GmERS1-1-CEND), which is indispensable for receptor function. Mechanistically, GmERS1-1-CEND scaffolds a trimeric complex with GmACR1 and GmCDK7, enforcing G2/M phase arrest, thereby decoupling cell division from canonical ethylene transcriptional responses. Strikingly, ethylene-induced cell cycle blockade during apple fruit maturation mirrors this pathway, suggesting deep conservation across angiosperms. Our work defines a receptor processing-dependent signaling axis that directly interlinks phytohormone perception with cell cycle control, proposing tunable targets (e.g., GmERS1-1 cleavage efficiency) for engineering crop architecture and productivity. In brief The cleaved C-terminal fragment of ethylene receptor GmERS1-1 enters into nucleus to inhibit cell cycle via interaction with GmACR1 in soybean. Highlights Mutating ethylene receptor GmERS1-1 significantly increases soybean yield in field. The cleaved C-terminal fragment of GmERS1-1 enters into the nucleus induced by ethylene and independent of CTR1. The C-terminal fragment has similar function to the full-length ethylene receptor GmERS1-1 to induce ethylene reaction in soybean and Arabidopsis . The C-terminal fragment of GmERS1-1 interacts with soybean GmACR1 to inhibit cell division.

Source: bioRxiv (Cold Spring Harbor Laboratory)

DOI: 10.64898/2026.10.07.757225