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 engineered plastid-targeted genetically encoded biosensors to visualize several phosphoinositide species (PI3P, PI4P, PI5P, PI(4,5)P2, PI(3,5)P2) within chloroplasts and confirmed their specificity via immunological assays. Co‑expression with PPI‑modifying enzymes revealed altered biosensor distribution, an association between PI3P and the chloroplast protein VIPP1, and that elevated PPI levels under stress change localization and increase drought sensitivity, highlighting PPIs in plant stress responses.