Diverse signals converge at MAPK cascades in plant.

Mitogen-activated protein kinases (MAPKs) are important signal transducing enzymes that connects diverse receptors/sensors to a wide range of cellular responses in mammals, yeasts and plants. In recent years, a large number of different components of plant MAPK cascades were isolated. Molecular and biochemical studies have revealed that plant MAPKs play important role in the response to a broad variety of biotic and abiotic stresses, including wounding, pathogen infection, temperature, drought, salinity, but also in the signaling of plant hormones and the cell division. This review briefly summaries the recent research results about the cross-talk and complexity of MAP kinase cascades in plant obtained from functional analyses.     

Mitogen-activated protein kinase cascades in plant signaling

Mitogen-activated protein kinase (MAPK) cascades are key signaling modules downstream of receptors/sensors that perceive either endogenously produced stimuli such as peptide ligands and damage-associated molecular patterns (DAMPs) or exogenously originated stimuli such as pathogen/microbe-associated molecular patterns (P/MAMPs), pathogen-derived effectors, and environmental factors. In this review, we provide a historic view of plant MAPK research and summarize recent advances in the establishment of MAPK cascades as essential components in plant immunity, response to environmental stresses, and normal growth and development. Each tier of the MAPK cascades is encoded by a small gene family, and multiple members can function redundantly in an MAPK cascade. Yet, they carry out a diverse array of biological functions in plants. How the signaling specificity is achieved has become an interesting topic of MAPK research. Future investigations into the molecular mechanism(s) underlying the regulation of MAPK activation including the activation kinetics and magnitude in response to a stimulus, the spatiotemporal expression patterns of all the components in the signaling pathway, and functional characterization of novel MAPK substrates are central to our understanding of MAPK functions and signaling specificity in plants.     

Jasmonate-dependent defense signaling in plant tissues

Depending on the stress type, plants activate various signal transduction pathways inducing the optimum defense process. This review is devoted to jasmonate (JA) dependent signaling involved in plant defense against biotic and abiotic stresses, including those determined by wounding, necrotrophic pathogens, pests, and herbivores. The sequence of major events of JA signaling is discussed. It is noted that JA signaling in plants is incorporated into a complex signaling network.     

Intercepting host MAPK signaling cascades by bacterial type III effectors

The evolutionarily conserved MAP kinase (MAPK) cascades play essential roles in plant and animal innate immunity. A recent explosion of research has uncovered a myriad of virulence strategies used by pathogenic bacteria to intercept MAPK signaling through diverse type III effectors injected into host cells. Here, we review the latest literature and discuss the various mechanisms that pathogenic bacteria use to manipulate host MAPK signaling cascades.     

Phospholipases in action during plant defense signaling

Eukaryotic organisms rely on intricate signaling networks to connect recognition of microbes with the activation of efficient defense reactions. Accumulating evidence indicates that phospholipids are more than mere structural components of biological membranes. Indeed, phospholipid-based signal transduction is widely used in plant cells to relay perception of extracellular signals. Upon perception of the invading microbe, several phospholipid hydrolyzing enzymes are activated that contribute to the establishment of an appropriate defense response. Activation of phospholipases is at the origin of the production of important defense signaling molecules, such as oxylipins and jasmonates, as well as the potent second messenger phosphatidic acid (PA), which has been shown to modulate the activity of a variety of proteins involved in defense signaling. Here, we provide an overview of recent reports describing the different plant phospholipase pathways that are activated during the establishment of plant defense reactions in response to pathogen attack.Key words: lipid signaling, PA, PLA, PLC, PLD, plant immunityIn plant cells, perception of pathogenic microbes largely relies on transmembrane pattern recognition receptors that specifically recognize highly conserved pathogen-derived molecules called PAMPs/MAMPs (pathogen-/microbial-associated molecular patterns), such as bacterial flagellin.¹ PAMP recognition by the plant leads to basal defense responses. A second layer of defense is based on the recognition of specific pathogen-derived molecules, called effectors, primarily by an additional class of plant cytoplasmic receptor proteins [nucleotide-binding leucine-rich repeat (NB-LRR) proteins] but also by protein receptors predicted to be located at the plasma membrane [receptor-like proteins (RLPs) and receptor-like kinases (RLKs)]. This recognition leads to the activation of plant immune responses that are frequently associated to the development of hypersensitive cell death (HR) at the inoculation site, which has been shown to contribute to plant resistance.²The activation of plant immunity involves a variety of early signaling events, including rapid accumulation of reactive oxygen species (ROS), changes in cellular ion fluxes, activation of protein kinase cascades, changes in gene expression and production of stress-related hormones.^3,4 During recent years, a substantial number of reports have also shown the importance of lipids and lipid-related molecules, including glycerolipids, sphingolipids, fatty acids, oxylipins, jasmonates and sterols, in the regulation of plant defense responses.⁵Phospholipids are more than structural components in biological membranes. Indeed, evidence that phospholipases and phospholipid-derived molecules are involved in plant signaling, and more particularly in plant immunity, is rapidly accumulating.^6,7 In plants, phosphatidic acid (PA) can be produced from phospholipids by phospholipase D (PLD) enzymes or from diacylyglycerol (DAG) by DAG kinases (DGKs) in the phospholipase C (PLC) pathway. PA is a potent secondary signal messenger molecule that modulates the activity of kinases, phosphatases, phospholipases and proteins involved in membrane-trafficking, Ca²⁺ signaling and the oxidative burst.^8,9 In addition, a growing body of evidence indicates that phospholipase A (PLA) [and related molecules such as lysophospholipids (LPLs) and free fatty acids (FFAs)] and phospholipase C (PLC) (and its related molecules DAG and DGK) play important roles in the control of the plant defense response to the attack by invading pathogens.⁷Here, we review the recent advances in understanding phospholipase-mediated signaling and its importance in the control of plant immune responses.     

Short- and long-distance signaling in plant defense

When encountering microbial pathogens, plant cells can recognize danger signals derived from pathogens, activate plant immune responses and generate cell-autonomous as well as non-cell-autonomous defense signaling molecules, which promotes defense responses at the infection site and in the neighboring cells. Meanwhile, local damages can result in the release of immunogenic signals including damage-associated molecule patterns and phytocytokines, which also serve as danger signals to potentiate immune responses in cells surrounding the infection site. Activation of local defense responses further induces the production of long-distance defense signals, which can move to distal tissue to activate systemic acquired resistance. In this review, we summarize current knowledge on various signaling molecules involved in short- and long-distance defense signaling, and emphasize the roles of regulatory proteins involved in the processes.     

p38 MAPK signalling cascades in inflammatory disease.

Inflammatory mediators released during acute and chronic diseases activate multiple intracellular signalling cascades including the mitogen-activated protein kinase (MAPK) signal transduction pathway, which plays a significant role in the recruitment of leukocytes to sites of inflammation. Stimulation of leukocytes by pro-inflammatory cytokines is known to result in the activation of the MAPK isoform p38. However, the functional consequences of p38 MAPK activation during leukocyte recruitment, including adhesion, migration and effector functions such as oxidative burst and degranulation, are only just beginning to be elucidated. Specific p38 inhibitors aimed at reducing the production of inflammatory mediators are now being developed, and might in the future provide more effective treatment for inflammatory diseases.     

Ethylene signaling pathway and MAPK cascades are required for AAL toxin-induced programmed cell death

Programmed cell death (PCD), known as hypersensitive response cell death, has an important role in plant defense response. The signaling pathway of PCD remains unknown. We employed AAL toxin and Nicotiana umbratica to analysis plant PCD. AAL toxin is a pathogenicity factor of the necrotrophic pathogen Alternaria alternata f. sp. lycopersici. N. umbratica is sensitive to AAL toxin, susceptible to pathogens, and effective in Tobacco rattle virus-based virus-induced gene silencing (VIGS). VIGS analyses indicated that AAL toxin-triggered cell death (ACD) is dependent upon the mitogen-activated protein (MAP) kinase kinase MEK2, which is upstream of both salicylic acid-induced protein kinase (SIPK) and wound-induced protein kinase (WIPK) responsible for ethylene (ET) synthesis. ET treatment of MEK2-silenced N. umbratica re-established ACD. In SIPK- and WIPK-silenced N. umbratica, ACD was compromised and ET accumulation was not observed. However, in contrast to the case of MEK2-silenced plants, ET treatment did not induce cell death in SIPK- and WIPK-silenced plants. This work showed that ET-dependent pathway and MAP kinase cascades are required in ACD. Our results suggested that MEK2-SIPK/WIPK cascades have roles in ET biosynthesis; however, SIPK and WIPK have other roles in ET signaling or another pathway leading to cell death by AAL toxin.     

MAPK cascades and major abiotic stresses

Plants have evolved with complex signaling circuits that operate under multiple conditions and govern numerous cellular functions. Stress signaling in plant cells is a sophisticated network composed of interacting proteins organized into tiered cascades where the function of a molecule is dependent on the interaction and the activation of another. In a linear scheme, the receptors of cell surface sense the stimuli and convey stress signals through specific pathways and downstream phosphorylation events controlled by mitogen-activated protein (MAP) kinases and second messengers, leading to appropriate adaptive responses. The specificity of the pathway is guided by scaffolding proteins and docking domains inside the interacting partners with distinctive structures and functions. The flexibility and the fine-tuned organization of the signaling molecules drive the activated MAP kinases into the appropriate location and connection to control and integrate the information flow. Here, we overview recent findings of the involvement of MAP kinases in major abiotic stresses (drought, cold and temperature fluctuations) and we shed light on the complexity and the specificity of MAP kinase signaling modules.     

Antagonistic interactions between two MAP kinase cascades in plant development and immune signaling

Mitogen‐activated protein kinase (MAPK) signaling plays important roles in diverse biological processes. In Arabidopsis, MPK3/MPK6, MKK4/MKK5, and the MAPKKK YODA (YDA) form a MAPK pathway that negatively regulates stomatal development. Brassinosteroid (BR) stimulates this pathway to inhibit stomata production. In addition, MPK3/MPK6 and MKK4/MKK5 also serve as critical signaling components in plant immunity. Here, we report that MAPKKK3/MAPKKK5 form a kinase cascade with MKK4/MKK5 and MPK3/MPK6 to transduce defense signals downstream of multiple plant receptor kinases. Loss of MAPKKK3/MAPKKK5 leads to reduced activation of MPK3/MPK6 in response to different pathogen‐associated molecular patterns (PAMPs) and increased susceptibility to pathogens. Surprisingly, developmental defects caused by silencing of YDA are suppressed in the mapkkk3 mapkkk5 double mutant. On the other hand, loss of YDA or blocking BR signaling leads to increased PAMP‐induced activation of MPK3/MPK6. These results reveal antagonistic interactions between a developmental MAPK pathway and an immune signaling MAPK pathway.