Calcium (Ca²⁺)/calmodulin (CaM)-dependent protein kinase (CCaMK) is an important positive regulator of abscisic acid (ABA) and abiotic stress signaling in plants and is believed to act upstream of mitogen-activated protein kinase (MAPK) in ABA signaling. However, it is unclear how CCaMK activates MAPK in ABA signaling. Here, we show that OsDMI3, a rice (Oryza sativa) CCaMK, directly interacts with and phosphorylates OsMKK1, a MAPK kinase (MKK) in rice, in vitro and in vivo. OsDMI3 was found to directly phosphorylate Thr-25 in the N-terminus of OsMKK1, and this Thr-25 phosphorylation is OsDMI3-specific in ABA signaling. The activation of OsMKK1 and its downstream kinase OsMPK1 is dependent on Thr-25 phosphorylation of OsMKK1 in ABA signaling. Moreover, ABA treatment induces phosphorylation in the activation loop of OsMKK1, and the two phosphorylations, in the N-terminus and in the activation loop, are independent. Further analyses revealed that OsDMI3-mediated phosphorylation of OsMKK1 positively regulates ABA responses in seed germination, root growth, and tolerance to both water stress and oxidative stress. Our results indicate that OsMKK1 is a direct target of OsDMI3, and OsDMI3-mediated phosphorylation of OsMKK1 plays an important role in activating the MAPK cascade and ABA signaling.

Trehalose-6-phosphate phosphatase (TPP) modulates the Trehalose-6-phosphate–trehalose balance, a key regulatory node in plant carbon sensing and stress resilience. However, its functional roles in vegetative crops such as potato (Solanum tuberosum, St) remains poorly understood. Here, we conducted a genome-wide identification of the StTPP gene family and identified nine distinct loci distributed across five chromosomes. Phylogenetic analysis categorized these loci into three clades, supported by conserved HAD-box motifs and distinct exon–intron structures. Family expansion was driven by segmental duplication under purifying selection. In silico promoter analysis revealed cis-elements responsive to hormones, light, and stress, while network modeling identified 64 transcription factors potentially involved in regulating StTPP expression. A biphasic transcriptional response was observed in the salt-tolerant cultivar Xisen6: rapid induction of StTPP2/3/9 early in salt exposure, followed by late repression of most members. Subcellular localization assays indicated that StTPP3 is present in the nucleus and cytosol, suggesting multifunctional roles. These findings suggest that StTPPs integrate developmental and environmental signals, providing a molecular basis for improving potato stress tolerance and yield stability.

Prefoldins (PFDs) are ubiquitous co-chaperone proteins that originated in archaea during evolution and are present in all eukaryotes, including yeast, mammals, and plants. Typically, prefoldin subunits form hexameric PFD complex (PFDc) that, together with class II chaperonins, mediate the folding of nascent proteins, such as actin and tubulin. In addition to functioning as a co-chaperone in cytoplasm, prefoldin subunits are also localized in the nucleus, which is essential for transcription and post-transcription regulation. However, the specific and critical roles of prefoldins in plants have not been well summarized. In this review, we present an overview of plant prefoldin and its related proteins, summarize the structure of prefoldin/prefoldin-like complex (PFD/PFDLc), and analyze the versatile landscape by prefoldin subunits, from cytoplasm to nucleus regulation. We also focus the specific role of prefoldin-mediated phytohormone response and global plant development. Finally, we overview the emerging prefoldin-like (PFDL) subunits in plants and the novel roles in related processes, and discuss the next direction in further studies.