The study reveals that REMORIN protein evolution is primarily driven by diversification of their conserved C-terminal domain, defining four major clades. Structural bioinformatics predicts a common membrane‑binding interface with diverse curvatures and lengths, and suggests that some REMs can form C‑terminal‑mediated oligomers, adding complexity to membrane organization.

The study identifies a conserved hydrophobic core within the coiled‑coil (CC) domain of helper NLRs (NRCs) that is essential for NRC4-mediated cell death and immunity. Structural and functional analyses show that this core regulates subcellular localization, oligomerization, and phospholipid association of NRC4, highlighting a novel mechanistic feature of NLR function.