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 authors used a bottom‑up thermodynamic modelling framework to investigate how plants decode calcium signals, starting from Ca2+ binding to EF‑hand proteins and extending to higher‑order decoding modules. They identified six universal Ca2+-decoding modules that can explain variations in calcium sensitivity among kinases and provide a theoretical basis for interpreting calcium signal amplitude and frequency in plant cells.

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.