Saline-alkali soil is a major environmental constraint impairing plant growth and crop productivity. In this study, we identified a Ca 21 sensor/kinase/plasma membrane (PM) H 1 -ATPase module as a central component conferring alkali tolerance in Arabidopsis (Arabidopsis thaliana). We report that the SCaBP3 (SOS3-LIKE CALCIUM BINDING PROTEIN3)/CBL7 (CALCINEURIN B-LIKE7) loss-of-function plants exhibit enhanced stress tolerance associated with increased PM H 1 -ATPase activity and provide fundamental mechanistic insights into the regulation of PM H 1 -ATPase activity. Consistent with the genetic evidence, interaction analyses, in vivo reconstitution experiments, and determination of H 1 -ATPase activity indicate that interaction of the Ca 21 sensor SCaBP3 with the C-terminal Region I domain of the PM H 1 -ATPase AHA2 (Arabidopsis thaliana PLASMA MEMBRANE PROTON ATPASE2) facilitates the intramolecular interaction of the AHA2 C terminus with the Central loop region of the PM H 1 -ATPase to promote autoinhibition of H 1 -ATPase activity. Concurrently, direct interaction of SCaPB3 with the kinase PKS5 (PROTEIN KINASE SOS2-LIKE5) stabilizes the kinase-ATPase interaction and thereby fosters the inhibitory phosphorylation of AHA2 by PKS5. Consistently, yeast reconstitution experiments and genetic analysis indicate that SCaBP3 provides a bifurcated pathway for coordinating intramolecular and intermolecular inhibition of PM H 1 -ATPase. We propose that alkaline stress-triggered Ca 21 signals induce SCaBP3 dissociation from AHA2 to enhance PM H 1 -ATPase activity. This work illustrates a versatile signaling module that enables the stress-responsive adjustment of plasma membrane proton fluxes.
N-myristoylation and S-acylation promote protein membrane association, allowing regulation of membrane proteins. However, how widespread this targeting mechanism is in plant signaling processes remains unknown. Through bioinformatics analyses, we determined that among plant protein kinase families, the occurrence of motifs indicative for dual lipidation by N-myristoylation and S-acylation is restricted to only five kinase families, including the Ca -regulated CDPK-SnRK and CBL protein families. We demonstrated N-myristoylation of CDPK-SnRKs and CBLs by incorporation of radiolabeled myristic acid. We focused on CPK6 and CBL5 as model cases and examined the impact of dual lipidation on their function by fluorescence microscopy, electrophysiology and functional complementation of Arabidopsis mutants. We found that both lipid modifications were required for proper targeting of CBL5 and CPK6 to the plasma membrane. Moreover, we identified CBL5-CIPK11 complexes as phosphorylating and activating the guard cell anion channel SLAC1. SLAC1 activation by CPK6 or CBL5-CIPK11 was strictly dependent on dual lipid modification, and loss of CPK6 lipid modification prevented functional complementation of cpk3 cpk6 guard cell mutant phenotypes. Our findings establish the general importance of dual lipid modification for Ca signaling processes, and demonstrate their requirement for guard cell anion channel regulation.
Adverse variations of abiotic environmental cues that deviate from an optimal range impose stresses to plants. Abiotic stresses severely impede plant physiology and development. Consequently, such stresses dramatically reduce crop yield and negatively impact on ecosystem stability and composition. Physical components of abiotic stresses can be, for example, suboptimal temperature and osmotic perturbations, while representative chemical facets of abiotic stresses can be toxic ions or suboptimal nutrient availability. The sheer complexity of abiotic stresses causes a multitude of diverse components and mechanisms for their sensing and signal transduction. Ca 2+ , as a versatile second messenger, plays multifaceted roles in almost all abiotic stress responses in that, for a certain abiotic stress, Ca 2+ is not only reciprocally connected with its perception, but also multifunctionally ensures subsequent signal transduction. Here, we will focus on salt/osmotic stress and responses to altered nutrient availability as model cases to detail novel insights into the identity of components that link stress perception to Ca 2+ signal formation as well as on new insights into mechanisms of Ca 2+ signal implementation. Finally, we will deduce emerging conceptual consequences of these novel insights and outline arising avenues of future research on the role of Ca 2+ signaling in abiotic stress responses in plants.
Efficient allocation of the essential nutrient potassium (K+) is a central determinant of plant ion homeostasis and involves AKT2 K+ channels. Here, we characterize four AKT2 K+ channels from cotton and report that xylem and phloem expressed GhAKT2bD facilitates K+ allocation and that AKT2‐silencing impairs plant growth and development. We uncover kinase activity‐dependent activation of GhAKT2bD‐mediated K+ uptake by AtCBL4–GhCIPK1 calcium signalling complexes in HEK293T cells. Moreover, AtCBL4–AtCIPK6 complexes known to convey activation of AtAKT2 in Arabidopsis also activate cotton GhAKT2bD in HEK293T cells. Collectively, these findings reveal an essential role for AKT2 in the source‐sink allocation of K+ in cotton and identify GhAKT2bD as subject to complex regulation by CBL–CIPK Ca2+ sensor–kinase complexes.
Systemic signaling is an essential hallmark of multicellular life. Pathogen encounter occurs locally but triggers organ-scale and organismic immune responses. In plants, elicitor perception provokes systemically expanding Ca2+and H2O2signals conferring immunity. Here, we identify a Ca2+sensing bi-kinase module as becoming super-activated through mutual trans-phosphorylation and imposing synergistically enhanced NADPH oxidase activation. A combined two-layer bi-kinase/substrate phospho-code allows for sensitized signaling initiation already by near-resting elevations of Ca2+concentration at the infection site. Subsequently, it facilitates further signal wave proliferation with minimal amplitude requirement, triggering protective defense responses throughout the plant. Our study reveals how plants build and perpetuate trans-cellular immune signal proliferation while avoiding disturbance of ongoing cellular signaling along the path of response dissemination.
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