The study shows that maize plants carrying autophagy-defective atg10 mutations exhibit delayed flowering and significant reductions in kernel size, weight, and number, culminating in lower grain yield. Reciprocal crossing experiments reveal that the maternal genotype, rather than the seed genotype, primarily drives the observed kernel defects, suggesting impaired nutrient remobilization from maternal tissues during seed development.

The study introduced charge-altering mutations into the N‑terminal region of Lhcb2 in Arabidopsis thaliana lacking native Lhcb2 to assess how intrinsic charge affects LHCII phosphorylation, state‑transition efficiency, and PSI‑LHCII complex formation. The R2E mutation drastically reduced Lhcb1/2 phosphorylation, impaired state transitions, and prevented PSI‑LHCII assembly, whereas the Q9E mutation had no measurable impact, and neither mutation altered thylakoid ultrastructure. Residual state transitions in the R2E line suggest that other Stn7 substrates can partially compensate for the loss of Lhcb2 phosphorylation.

The study demonstrates that the plastid chaperone CLPC2, but not its paralogue CLPC1, is essential for Arabidopsis responsiveness to microbial volatile compounds and for normal seed and seedling development. Loss of CLPC2 alters the chloroplast proteome, affecting proteins linked to growth, photosynthesis, and embryogenesis, while overexpression of CLPC2 mimics CLPC1 deficiency, highlighting distinct functional roles within the CLP protease complex.

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 reveals that brassinosteroids activate phosphoenolpyruvate carboxykinase (PCK) by promoting dephosphorylation of conserved Ser-62 and Thr-66 residues, a process antagonized by the GSK3-like kinase BIN2. BR‑deficient Arabidopsis mutants exhibit reduced PCK activity, while phospho‑blocking mutations confer BR‑independent activation and enhanced seedling growth, and similar regulatory mechanisms are observed in maize and sorghum leaves.

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 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 demonstrates that ABI5‑Binding Proteins (AFPs) interact with multiple components of the core ABA signaling pathway and serve as substrates for SnRK2 kinases and PP2C phosphatases, linking them to MAP kinases and 14‑3‑3 proteins. Phosphorylation of AFP2, promoted by ABA, stabilizes the protein and influences its subcellular localization, thereby modulating its ability to inhibit ABA responses during seed germination.

The study identifies the RNA‑binding protein AtG3BP1 as a phosphorylation target of MAPKs MPK3, MPK4, and MPK6 at Ser257 in Arabidopsis thaliana and shows that this modification promotes susceptibility to bacterial pathogens, suppresses ROS accumulation and salicylic acid biosynthesis, and maintains stomatal opening. Phospho‑mimic and phospho‑dead mutants reveal that phosphorylation stabilizes AtG3BP1 by preventing proteasomal degradation, highlighting a novel post‑translational control layer in plant immunity.

The study identifies a moss‑specific fusion protein, Rosetta NATD‑MAPK 1 (RAK1), that combines a MAPK domain with an N‑acetyltransferase and demonstrates that its acetyltransferase activity is enhanced upon MAPK activation. Knockout of RAK1 impairs the 2D‑to‑3D developmental transition in Physcomitrium patens, and mass‑spectrometry reveals associated changes in acetylation and phosphorylation linked to metabolic reprogramming.