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 authors compiled and standardized published data on Rubisco dark inhibition for 157 flowering plant species, categorizing them into four inhibition levels and analyzing phylogenetic trends. Their meta‑analysis reveals a complex, uneven distribution of inhibition across taxa, suggesting underlying chloroplast microenvironment drivers and providing a new resource for future photosynthesis improvement efforts.

The study evaluated a transgenic soybean line (VPZ-34A) expressing Arabidopsis VDE, PsbS, and ZEP for combined improvements in light‑use efficiency and carbon assimilation under ambient and elevated CO2 in a FACE experiment. While VPZ‑34A showed enhanced maximum quantum efficiency of PSII under fluctuating light, it did not increase carbon assimilation efficiency or yield, and transcriptome analysis revealed limited gene expression changes. The results suggest that VPZ‑mediated photosynthetic gains are insufficient to boost productivity under elevated CO2.

The study identifies EPP1 as a fourth, conserved component of the ancestral common symbiosis pathway required for intracellular plant–microbe interactions, showing that its loss impairs arbuscular mycorrhizal colonization across diverse plant clades. EPP1 is phosphorylated by the plasma‑membrane receptor SYRMK, and this modification is essential for downstream activation of the nuclear kinase CCaMK, positioning EPP1 upstream in the signaling cascade.

The study identifies Early Phosphorylated Protein 1 (EPP1) as a pivotal cytoplasmic mediator that links the SYMRK receptor to downstream symbiotic signaling, with phosphorylation of a key serine residue being both necessary and sufficient for nodule formation. Structural and functional analyses confirm the SYMRK‑EPP1 complex, and engineered synthetic interaction of these proteins can induce nodule organogenesis without bacterial presence.