The intracellular potassium (K(+) ) homeostasis, which is crucial for plant survival in saline environments, is modulated by K(+) channels and transporters. Some members of the high-affinity K(+) transporter (HAK) family are believed to function in the regulation of plant salt tolerance, but the physiological mechanisms remain unclear. Here, we report a significant inducement of OsHAK21 expression by high-salinity treatment and provide genetic evidence of the involvement of OsHAK21 in rice salt tolerance. Disruption of OsHAK21 rendered plants sensitive to salt stress. Compared with the wild type, oshak21 accumulated less K(+) and considerably more Na(+) in both shoots and roots, and had a significantly lower K(+) net uptake rate but higher Na(+) uptake rate. Our analyses of subcellular localizations and expression patterns showed that OsHAK21 was localized in the plasma membrane and expressed in xylem parenchyma and individual endodermal cells (putative passage cells). Further functional characterizations of OsHAK21 in K(+) uptake-deficient yeast and Arabidopsis revealed that OsHAK21 possesses K(+) transporter activity. These results demonstrate that OsHAK21 may mediate K(+) absorption by the plasma membrane and play crucial roles in the maintenance of the Na(+) /K(+) homeostasis in rice under salt stress.

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H(2)O(2) is an essential signal in absicic acid (ABA)-induced stomatal closure. It can be synthesized by several enzymes in plants. In this study, the roles of copper amine oxidase (CuAO) in H(2)O(2) production and stomatal closure were investigated. Exogenous ABA stimulated apoplast CuAO activity, increased H(2)O(2) production and [Ca(2+)](cyt) levels in Vicia faba guard cells, and induced stomatal closure. These processes were impaired by CuAO inhibitor(s). In the metabolized products of CuAO, only H(2)O(2) could induce stomatal closure. By the analysis of enzyme kinetics and polyamine contents in leaves, putrescine was regarded as a substrate of CuAO. Putrescine showed similar effects with ABA on the regulation of H(2)O(2) production, [Ca(2+)](cyt) levels, as well as stomatal closure. The results suggest that CuAO in V. faba guard cells is an essential enzymatic source for H(2)O(2) production in ABA-induced stomatal closure via the degradation of putrescine. Calcium messenger is an important intermediate in this process.

Remodeling of auxin distribution during the integration of plant growth responses with the environment requires the precise control of auxin influx and efflux transporters. The plasma membrane-localized PIN-FORMED (PIN) proteins facilitate auxin efflux from cells, and their activity is regulated by reversible phosphorylation. How PIN modulates plant cellular responses to external stresses and whether its activity is coordinated by phospholipids remain unclear. Here, we reveal that, in Arabidopsis (Arabidopsis thaliana), the phosphatidic acid (PA)-regulated PINOID (PID) kinase is a crucial modulator of PIN2 activity and auxin redistribution in response to salt stress. Under salt stress, loss of phospholipase D function impaired auxin redistribution and resulted in markedly reduced primary root growth; these effects were reversed by exogenous PA. The phospholipase D-derived PA interacted with PID and increased PID-dependent phosphorylation of PIN2, which activated auxin efflux and altered auxin accumulation, promoting root growth when exposed to salt stress. Ablation of the PA binding motif not only diminished PID accumulation at the plasma membrane but also abolished PA-promoted PID phosphorylation of PIN2 and its function in coping with salt stress; however, this ablation did not affect inflorescence and cotyledon development or PIN2-dependent gravitropic and halotropic responses. Our data indicate a role for PA in coupling extracellular salt signaling to PID-directed PIN2 phosphorylation and polar auxin transport, highlighting the importance of lipid-protein interactions in the spatiotemporal regulation of auxin signaling.

In animal cells, phospholipase C (PLC) isoforms predominantly hydrolyze phosphatidylinositol-4,5-biphosphates [PtdIns(4,5)P ] into the second messengers diacylglycerol (DAG) and inositol 1,4,5-trisphosphate [Ins(1,4,5)P ] to regulate diverse biological processes. By contrast, the molecular mechanisms and physiological significance of PLC signaling in plants still awaits full elucidation. Here, we identified a rice (Oryza sativa cv) PI-PLC, OsPLC1, which preferred to hydrolyze phosphatidylinositol-4-phosphate (PtdIns4P) and elicited stress-induced Ca signals regulating salt tolerance. Analysis by ion chromatography revealed that the concentration of PtdIns4P was c. 28 times of that of PtdIns(4,5)P in shoots. OsPLC1 not only converted PtdIns(4,5)P but also - and even more efficiently - converted PtdIns4P into DAG and Ins(1,4,5)P in vitro and in vivo. Salt stress induced the recruitment of OsPLC1 from cytoplasm to plasma membrane, where it hydrolyzed PtdIns4P. The stress-induced Ca signaling was dependent on OsPLC1, and the PLC-mediated Ca signaling was essential for controlling Na accumulation in leaf blades, thus establishing whole plant salt tolerance. Our work identifies a conversion pathway and physiological function for PtdIns4P pools in rice and reveals the connection between phosphoinositides and Ca signals mediated by PLC during salt stress responses.