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 generated deep proteome and phosphoproteome datasets from guard cell‑enriched tissue to examine how phosphorylation regulates stomatal movements. Comparative analysis revealed increased phosphorylation of endomembrane trafficking and vacuolar proteins in closed stomata, supporting a role for phospho‑regulated trafficking in stomatal dynamics.

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.