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 examined how osmotic stress and cytosolic Ca²⁺ signaling regulate autophagy in plants by monitoring the dynamics of RFP‑tagged ATG8i. Both stimuli altered the accumulation of RFP‑ATG8i‑labeled autophagosomes in an organ‑specific way, and colocalization with the ER marker HDEL indicated that ATG8i participates in ER‑phagy during stress.

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.

The study reveals that the bacterial pathogen Pseudomonas syringae suppresses host plant translation by targeting processing bodies (P‑bodies) through two liquid-like effectors, linking this repression to the ER stress response. It further demonstrates that autophagic clearance of P‑bodies is essential for balancing translationally active and inactive mRNAs, uncovering new connections among translation, ER stress, and autophagy during plant immunity.