Agricultural productivity worldwide is subject to increasing environmental constraints, particularly to drought and salinity due to their high magnitude of impact and wide distribution. Traditional breeding programs trying to improve abiotic stress tolerance have had some success, but are limited by the multigenic nature of the trait. Tolerant plants such as Craterostigma plantagenium, Mesembryanthemum crystallinum, Thellungiella halophila and other hardy plants could be valuable tools to dissect the extreme tolerance nature. In the last decade, Arabidopsis thaliana, a genetic model plant, has been extensively used for unravelling the molecular basis of stress tolerance. Arabidopsis also proved to be extremely important for assessing functions for individual stress-associated genes due to the availability of knock-out mutants and its amenability for genetic transformation. In this review, the responses of plants to salt and water stress are described, the regulatory circuits which allow plants to cope wit...

Drought and Salt Tolerance in Plants

One-fifth of irrigated agriculture is adversely affected by soil salinity. Hence, developing salt-tolerant crops is essential for sustaining food production. Progress in breeding for salt-tolerant crops has been hampered by the lack of understanding of the molecular basis of salt tolerance and lack of availability of genes that confer salt tolerance. Genetic evidence suggests that perception of salt stress leads to a cytosolic calcium-signal that activates the calcium sensor protein SOS3. SOS3 binds to and activates a ser/thr protein kinase SOS2. The activated SOS2 kinase regulates activities of SOS1, a plasma membrane Na + /H + antiporter, and NHX1, a tonoplast Na + /H + anti-porter. This results in Na + efflux and vacuolar compartmentation. A putative osmosensory histidine kinase (AtHKI)-MAPK cascade probably regulates osmotic homeostasis and ROS scavenging. Osmotic stress and ABA (abscisic acid)-mediated regulation of LEA (late-embryogenesis-abundant)-type proteins also play important roles in plant salt tolerance. Genetic engineering of ion transporters and their regulators, and of the CBF (C-repeat-binding factor) regulons, holds promise for future development of salt-tolerant crops.

Understanding and Improving Salt Tolerance in Plants

Mitogen-activated protein kinase cascades in plants: a new nomenclature

The perception of abiotic stresses and signal transduction to switch on adaptive responses are critical steps in determining the survival and reproduction of plants exposed to adverse environments. Plants have stress-specific adaptive responses as well as responses which protect the plants from more than one environmental stress. There are multiple stress perception and signalling pathways, some of which are specific, but others may cross-talk at various steps. Recently, progress has been made in identifying components of signalling pathways involved in salt, drought and cold stresses. Genetic analysis has defined the Salt-Overly-Sensitive (SOS) pathway, in which a salt stress-induced calcium signal is probably sensed by the calcium-binding protein SOS3 which then activates the protein kinase SOS2. The SOS3‐SOS2 kinase complex regulates the expression and activity of ion transporters such as SOS1 to reestablish cellular ionic homeostasis under salinity. The ICE1 (Inducer of CBF Expression 1)‐CBF (CRepeat Binding Protein) pathway is critical for the regulation of the cold-responsive transcriptome and acquired freezing tolerance, although at present the signalling events that activate the ICE1 transcription factor during cold stress are not known. Both ABAdependent and -independent signalling pathways appear to be involved in osmotic stress tolerance. Components of mitogen-activated protein kinase (MAPK) cascades may act as converging points of multiple abiotic as well as biotic stress signalling pathways. Forward and reverse genetic analysis in combination with expression profiling will continue to uncover many signalling components, and biochemical characterization of the signalling complexes will be required to determine specificity and crosstalk in abiotic stress signalling pathways.

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Molecular genetic perspectives on cross‐talk and specificity in abiotic stress signalling in plants

Eukaryotic mitogen-activated protein kinase (MAPK) cascades have evolved to transduce environmental and developmental signals into adaptive and programmed responses MAPK cascades relay and amplify signals via three types of reversibly phosphorylated kinases leading to the phosphorylation of substrate proteins, whose altered activities mediate a wide array of responses, including changes in gene expression Cascades may share kinase components, but their signaling specificity is maintained by spaciotemporal constraints and dynamic protein-protein interactions and by mechanisms that include crossinhibition, feedback control, and scaffolding Plant MAPK cascades regulate numerous processes, including stress and hormonal responses, innate immunity, and developmental programs Genetic analyses have uncovered several predominant MAPK components shared by several of these processes including the Arabidopsis thaliana MAPKs MPK3, 4, and 6 and MAP2Ks MKK1, 2, 4, and 5 Future work needs to focus on identifying substrates of MAPKs, and on understanding how specificity is achieved among MAPK signaling pathways

Mitogen-Activated Protein Kinase Signaling in Plants

CTR1 encodes a negative regulator of the ethylene response pathway in Arabidopsis thaliana. The C-terminal domain of CTR1 is similar to the Raf family of protein kinases, but its first two-thirds encodes a novel protein domain. We used a variety of approaches to investigate the function of these two CTR1 domains. Recombinant CTR1 protein was purified from a baculoviral expression system, and shown to possess intrinsic Ser/Thr protein kinase activity with enzymatic properties similar to Raf-1. Deletion of the N-terminal domain did not elevate the kinase activity of CTR1, indicating that, at least in vitro, this domain does not autoinhibit kinase function. Molecular analysis of loss-of-function ctr1 alleles indicated that several mutations disrupt the kinase catalytic domain, and in vitro studies confirmed that at least one of these eliminates kinase activity, which indicates that kinase activity is required for CTR1 function. One missense mutation, ctr1-8, was found to result from an amino acid substitution within a new conserved motif within the N-terminal domain. Ctr1-8 has no detectable effect on the kinase activity of CTR1 in vitro, but rather disrupts the interaction with the ethylene receptor ETR1. This mutation also disrupts the dominant negative effect that results from overexpression of the CTR1 amino-terminal domain in transgenic Arabidopsis. These results suggest that CTR1 interacts with ETR1 in vivo, and that this association is required to turn off the ethylene-signaling pathway.

https://www.onlinelibrary.wiley.com/doi/pdf/10.1046/j.1365-313X.2003.01620.x

Biochemical and functional analysis of CTR1, a protein kinase that negatively regulates ethylene signaling in Arabidopsis.

The modulation of mitogen-activated protein kinase (MAPK) activity regulates many intracellular signaling processes. In animal and yeast cells, MAP kinases are activated via phosphorylation by the dual-specificity kinase MEK (MAP kinase kinase). Several plant homologs of MEK and MAPK have been identified, but the biochemical events underlying the activation of plant MAPKs remain unknown. We describe the in vitro activation of an Arabidopsis homolog of MAP kinase, ATMPK4. ATMPK4 was phosphorylated in vitro by an Arabidopsis MEK homolog, AtMEK1. This phosphorylation occurred principally on threonine (Thr) residues and resulted in elevated ATMPK4 kinase activity. A second Arabidopsis MEK isoform, ATMAP2Kα, failed to phosphorylate ATMPK4 in vitro. Tyr dephosphorylation by the Arabidopsis Tyr-specific phosphatase AtPTP1 resulted in an almost complete loss of ATMPK4 activity. Immunoprecipitates of Arabidopsis extracts with anti-ATMPK4 antibodies displayed myelin basic protein kinase activity that was sensitive to treatment with AtPTP1. These results demonstrate that a plant MEK can phosphorylate and activate MAPK, and that Tyr phosphorylation is critical for the catalytic activity of MAPK in plants. Surprisingly, in contrast to the animal enzymes, AtMEK1 may not be a dual-specificity kinase but, rather, the required Tyr phosphorylation on ATMPK4 may result from autophosphorylation.

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Hui Li

Papers

Biochemical and functional analysis of CTR1, a protein kinase that negatively regulates ethylene signaling in Arabidopsis.

ATMPK4, an Arabidopsis Homolog of Mitogen-Activated Protein Kinase, Is Activated in Vitro by AtMEK1 through Threonine Phosphorylation