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.

Reduced activity of methylthioadenosine (MTA) nucleosidase causes MTA over‑accumulation in reproductive tissues, leading to lowered cysteine, methionine, and S‑adenosylmethionine levels and altered sulfur and energy metabolism. These metabolic disturbances trigger misregulation of cell‑cycle progression, widespread down‑regulation of developmental genes, and genome‑wide changes in DNA methylation patterns, highlighting the extensive role of MTA recycling in plant growth and methyl‑index maintenance.