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.

Using a microfluidic valve rootchip, the study simultaneously tracked ROS and calcium dynamics in compressed roots and found three kinetic phases linking mechanosensitive channel activity, NADPH oxidase‑dependent ROS accumulation, and secondary calcium influx. Pharmacological inhibition revealed that a fast calcium response is mediated by plasma‑membrane mechanosensitive channels, while a slower calcium increase is driven by ROS production.

The study characterizes a plasma membrane-localized, calcium‑permeable force‑gated channel named Rapid Mechanically Activated (RMA) in plants, using patch‑clamp and pressure‑clamp to elucidate its rapid activation, inactivation, and irreversible adaptation upon repeated mechanical stimulation. Kinetic modeling shows the channel functions as a pass‑band filter for frequencies between 10 Hz and 1 kHz, supporting its role in transducing high‑frequency mechano‑stimuli such as insect vibrations.