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In addition to mediating cell adhesion, many cell adhesion molecules act as tumor suppressors. These proteins are capable of restricting cell growth mainly through contact inhibition. Alterations of these cell adhesion molecules are a common event in cancer. The resulting loss of cell-cell and/or cell-extracellular matrix adhesion promotes cell growth as well as tumor dissemination. Therefore, it is conventionally accepted that cell adhesion molecules that function as tumor suppressors are also involved in limiting tumor cell migration. Paradoxically, in 2005, we identified an immunoglobulin superfamily cell adhesion molecule hepaCAM that is able to suppress cancer cell growth and yet induce migration. Almost concurrently, CEACAM1 was verified to co-function as a tumor suppressor and invasion promoter. To date, the reason and mechanism responsible for this exceptional phenomenon remain unclear. Nevertheless, the emergence of these intriguing cell adhesion molecules with conflicting roles may open a new chapter to the biological significance of cell adhesion molecules.Key words: hepaCAM, cell adhesion molecules, tumor suppressor, migration, E-cadherin, CADM1, integrin α7, CEACAM1It is well known that many cell adhesion molecules function as tumor suppressors (reviewed in ref. 1). These molecules exert their tumor suppressive effect mainly through cell-adhesion-mediated contact inhibition. Cell adhesion molecules allow cells to communicate with one another or to the extracellular environment by mediating cell-cell or cell-extracellular matrix (ECM) interactions (reviewed in refs. 2 and 3). Broadly, these proteins can be classified into five families including immunoglobulin superfamily, integrins, cadherins, selectins and CD44. Apart from participating in the development and maintenance of tissue architecture, cell adhesion molecules serve as cell surface receptors critical for capturing, integrating and transmitting signals from the extracellular milieu to the cell interior (reviewed in refs. 2 and 3). These signaling events are vital for the regulation of a wide variety of cellular functions including embryogenesis, immune and inflammatory responses, tissue repair, cell migration, differentiation, proliferation and apoptosis. Alterations of these cell adhesion molecules are a common event in cancer (reviewed in refs. 1, 2, 4 and 5). The disrupted cell-cell or cell-ECM adhesion significantly contributes to uncontrolled cell proliferation and progressive distortion of normal tissue architecture. More importantly, changes in cell adhesion molecules play a causal role in tumor dissemination. Loss of cell adhesion contacts allows malignant cells to detach and to escape from the primary mass. Gaining a more motile and invasive phenotype, these cells break down the ECM and eventually invade and metastasize to distal organs.Based on the above understanding, it is conventionally accepted that cell adhesion molecules with tumor suppressor activity, when expressed in cancer cells, are able to exert inhibitory effect on cell motility. The ability of cells in migration/motility is a prerequisite for cancer invasion and metastasis (reviewed in refs. 1 and 5). Indeed, a number of cell adhesion molecule-tumor suppressors have been reported to be capable of reducing cell migration. The most classical example is E-cadherin, a calcium-dependent cell adhesion molecule. E-cadherin is expressed exclusively in epithelial cells and its expression is commonly suppressed in tumors of epithelial origins. The cytoplasmic domain of E-cadherin interacts with catenins to establish an intracellular linkage with the actin cytoskeleton (reviewed in ref. 6). The assembly of E-cadherin with the cytoskeleton via catenins at the sites of adherens junctions is important for the stabilization of cell-cell adhesions. Disruption of E-cadherin-mediated cell-cell adhesion, due to loss of expression or function of E-cadherin and/or catenins, is assocated with tumor development and progression (reviewed in ref. 7). Forced expression of E-cadherin in several cancer cell lines not only slows down cell growth8,9 but also significantly reduces the invasiveness of the cells.10,11 On the other hand, inhibition of E-cadherin by function-blocking antibodies and antisense RNA restores the invasiveness in non-invasive transformed cells.11 Furthermore, using a transgenic mouse model of pancreatic beta-cell carcinogenesis, it has been demonstrated that E-cadherin-mediated cell adhesion is important in preventing the transition from well differentiated adenoma to invasive carcinoma.12Cell adhesion molecule 1 (CADM1), another example, has also been implicated in cancer progression. CADM1 is a member of the immunoglobulin superfamily and mediates cell-cell adhesion.13 The molecule associates with the actin cytoskeleton via the differentially expressed in adenocarcinoma of the lung (DAL1) protein; and the formation of CADM1-DAL1 complex is dependent on the integrity of actin cytoskeleton.14 Inactivation of the CADM1 and/or DAL1 gene usually through methylation has been reported in diverse human cancers.15,16 A paper by Ito et al. showed that restoration of CADM1 expression in esophageal squamous cell carcinoma cells not only suppresses cell growth, but also retards cell motility and invasion.16In contrast to E-cadherin and CADM1, integrin α7 is a cell-ECM adhesion molecule which also possesses tumor suppressor activity. Ren et al. showed that integrin α7 gene is mutated in several human malignances; and the mutations are associated with an increase in cancer recurrence.17 Forced expression of integrin α7 in integrin α7-deficient leiomyosarcoma cells results in decreased colony formation and slower cell motility. Conversely, knockdown of integrin α7 in lung cancer cells expressing wild-type integrin α7 increases the colony number and cell motility rate. In addition, the researchers revealed that mice bearing xenograft tumors overexpressing integrin α7 have reduced tumor size with no obvious metastasis.In 2005, we first reported the identification of a cell adhesion molecule belonging to the immunoglobulin superfamily, designated as hepaCAM.18 To date, we have shown that the gene is frequently downregulated in a variety of human cancers.18,19 Re-expression of hepaCAM in the hepatocellular carcinoma HepG2 cells18 and breast cancer MCF7 cells19 inhibits colony formation and retards cell proliferation. In addition, expression of hepaCAM in MCF7 cells results in cell cycle arrest at the G2/M phase and cellular senescence. Concurrently, the expression of several senescence-associated proteins including p53, p21 and p27 is enhanced. Moreover, downregulation of p53 by p53-specific small interfering RNA in cells expressing hepaCAM clearly reduces p21 without changing p27 and alleviates senescence, indicating that hepaCAM induces senescence through a p53/p21-dependent pathway.19 Together, the data suggest that hepaCAM is a tumor suppressor. Interestingly, the expression of hepaCAM in both HepG2 and MCF7 cells stimulates both cell-ECM adhesion and cell migration.18,20,21 The function of hepaCAM as a tumor suppressor in cell migration is contradictory to other cell adhesion molecule-tumor suppressors. Noteworthily, hepaCAM-mediated cell motility is evidenced by its direct interaction with the actin cytoskeleton.21Evidences are currently emerging to support the contradictory roles of cell adhesion molecules that both inhibit cell growth and promote cell motility when restored in cancer cells. In addition to hepaCAM, the immunoglobulin superfamily carcinoembryonic antigen-related cell adhesion molecule 1 (CEACAM1) is implicated to function as a tumor suppressor and a metastasis promoter. The characteristics and functions of CEACAM1 have been demonstrated in individual reports. CEACAM1 is frequently downregulated or dysregulated in multiple human tumors,22–25 and is capable of suppressing cell growth and inducing apoptosis.26–28 Ebrahimnejad et al. demonstrated that exogenous expression of CEACAM1 enhances melanoma cell invasion and migration; and this enhanced motility can be reverted by anti-CEACAM antibodies.29 The ability of CEACAM to co-stimulate tumor suppression and invasion was finally established by Liu et al. in restricting thyroid cancer growth but promoting invasiveness.30 Introduction of CEACAM1 into CEACAM1-deficient thyroid cancer cells results in G1/S phase cell cycle arrest accompanied by elevated p21 expression and diminished Rb phosphorylation. Overexpression of CEACAM1 also increases cell-ECM adhesion and promotes cell migration and tumor invasiveness. In xenografted mice, CEACAM1 expression results in reduced tumor growth but increased tumor invasiveness. Conversely, silencing of endogenous CEACAM1 accelerates tumor growth and suppresses invasiveness.30It is an exciting issue to address why a cell adhesion molecule is able to suppress tumor growth yet promote tumor progression. Could there be a molecular switch that controls the functions of the gene between a tumor suppressor and a migration promoter in cancer or are the functions executed simultaneously? The expression level, the extracellular cues as well as the interacting partners of the cell adhesion molecules may likely play a critical role in regulating its functions. The question is under what circumstances these factors come into play. To answer all these questions, and maybe more, on the intriguing findings of these proteins, more extensive and intensive experimentation is required. Nevertheless, it is obvious that the emergence of these cell adhesion molecules that function in a contradictory manner opens a new chapter to the biological significance of cell adhesion molecules. 相似文献
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Strigolactones (SLs) have been recently identified as a new group of plant hormones or their derivatives thereof, shown to play a role in plant development. Evolutionary forces have driven the development of mechanisms in plants that allow adaptive adjustments to a variety of different habitats by employing plasticity in shoot and root growth and development. The ability of SLs to regulate both shoot and root development suggests a role in the plant''s response to its growth environment. To play this role, SL pathways need to be responsive to plant growth conditions, and affect plant growth toward increased adaptive adjustment. Here, the effects of SLs on shoot and root development are presented, and possible feedback loops between SLs and two environmental cues, light and nutrient status, are discussed; these might suggest a role for SLs in plants'' adaptive adjustment to growth conditions.Key words: strigolactones, light, nutrient status, root, shoot, branching, lateral roots, root hairsStrigolactones (SLs) are carotenoid-derived terpenoid lactones suggested to stem from the carotenoid pathway1 via the activity of various oxygenases.2,3 SLs production has been demonstrated in both monocotyledons and eudicotyledons (reviewed in ref. 4), suggesting their presence in many plant species.5 SLs are synthesized mainly in the roots and in some parts of the stem and then move towards the shoot apex (reviewed ref. 7).6,8,9SLs were first characterized more than 40 years ago as germination stimulants of the parasitic plants Striga and Orobanche and later, as stimulants of arbuscular mycorrhiza hyphal branching as well (reviewed in ref. 4, 10–13). Recently, SLs or derivatives thereof, have been identified as a new group of plant hormones, shown to play a role in inhibition of shoot branching,2,3,8,9 thereby affecting shoot architecture; more recently they have also been shown to affect root growth by affecting auxin efflux.14Plants have developed mechanisms that allow adaptive adjustments to a variety of different habitats by employing plasticity in their growth and development.15 Shoot architecture is affected by environmental cues, such as light quality and quantity and nutrient status.16–19 Root-system architecture and development are affected by environmental conditions such as nutrient availability (reviewed in ref. 20, 21). At the same time, plant hormones are known to be involved in the regulation of plant growth, development and architecture (reviewed in ref. 22–24) and to be mediators of the effects of environmental cues on plant development; one classic example is auxin''s role in the plant''s shade-avoidance response (reviewed in ref. 25).The ability of SLs to regulate shoot and root development suggests that these phytohormones also have a role in the plant''s growth response to its environment. To play this putative role, SL pathways need to be responsive to plant growth conditions, and affect plant growth toward enhancing its adaptive adjustment. The present review examines the SLs'' possible role in adaptive adjustment of the plant''s response to growth conditions, by discussing their effect on plant development and the possible associations and feedback loops between SLs and two environmental cues: light and nutrient status. 相似文献
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Cell migration during wound healing is a complex process that involves the expression of a number of growth factors and cytokines. One of these factors, transforming growth factor-beta (TGFβ) controls many aspects of normal and pathological cell behavior. It induces migration of keratinocytes in wounded skin and of epithelial cells in damaged cornea. Furthermore, this TGFβ-induced cell migration is correlated with the production of components of the extracellular matrix (ECM) proteins and expression of integrins and matrix metalloproteinases (MMPs). MMP digests ECMs and integrins during cell migration, but the mechanisms regulating their expression and the consequences of their induction remain unclear. It has been suggested that MMP-14 activates cellular signaling processes involved in the expression of MMPs and other molecules associated with cell migration. Because of the manifold effects of MMP-14, it is important to understand the roles of MMP-14 not only the cleavage of ECM but also in the activation of signaling pathways.Key words: wound healing, migration, matrix metalloproteinase, transforming growth factor, skin, corneaWound healing is a well-ordered but complex process involving many cellular activities including inflammation, growth factor or cytokine secretion, cell migration and proliferation. Migration of skin keratinocytes and corneal epithelial cells requires the coordinated expression of various growth factors such as platelet-derived growth factor (PDGF), fibroblast growth factor (FGF), transforming growth factor (TGF), keratinocyte growth factor (KGF), hepatocyte growth factor (HGF), insulin-like growth factor (IGF), epidermal growth factor (EGF), small GTPases, and macrophage stimulating protein (reviewed in refs. 1 and 2). The epithelial cells in turn regulate the expression of matrix metalloproteinases (MMPs), extracellular matrix (ECM) proteins and integrins during cell migration.1,3,4 TGF-β is a well-known cytokine involved in processes such as cell growth inhibition, embryogenesis, morphogenesis, tumorigenesis, differentiation, wound healing, senescence and apoptosis (reviewed in refs. 5 and 6). It is also one of the most important cytokines responsible for promoting the migration of skin keratinocytes and corneal epithelial cells.3,6,7TGFβ has two quite different effects on skin keratinocytes: it suppresses their multiplication and promotes their migration. The TGFβ-induced cell growth inhibition is usually mediated by Smad signaling, which upregulates expression of the cell cycle inhibitor p21WAF1/Cip1 or p12CDK2-AP1 in HaCaT skin keratinocyte cells and human primary foreskin keratinocytes.8,9 Keratinocyte migration in wounded skin is associated with strong expression of TGFβ and MMPs,1 and TGFβ stimulates the migration of manually scratched wounded HaCaT cells.10 TGFβ also induces cell migration and inhibits proliferation of injured corneal epithelial cells, whereas it stimulates proliferation of normal corneal epithelial cells via effects on the MAPK family and Smad signaling.2,7 Indeed, skin keratinocytes and corneal epithelial cells display the same two physiological responses to TGFβ during wound healing; cell migration and growth inhibition. However as mentioned above, TGFβ has a different effect on normal cells. For example, it induces the epithelial to mesenchymal transition (EMT) of normal mammary cells and lens epithelial cells.11,12 It also promotes the differentiation of corneal epithelial cells, and induces the fibrosis of various tissues.2,6The MMPs are a family of structurally related zinc-dependent endopeptidases that are secreted into the extracellular environment.13 Members of the MMP family have been classified into gelatinases, stromelysins, collagenases and membrane type-MMPs (MT-MMPs) depending on their substrate specificity and structural properties. Like TGFβ, MMPs influence normal physiological processes including wound healing, tissue remodeling, angiogenesis and embryonic development, as well as pathological conditions such as rheumatoid arthritis, atherosclerosis and tumor invasion.13,14The expression patterns of MMPs during skin and cornea wound healing are well studied. In rats, MMP-2, -3, -9, -11, -13 and -14 are expressed,15 and in mice, MMP-1, -2, -3, -9, -10 and -14 are expressed during skin wound healing.1 MMP-1, -3, -7 and -12 are increased in corneal epithelial cells during Wnt 7a-induced rat cornea wound healing.16 Wound repair after excimer laser keratectomy is characterized by increased expression of MMP-1, -2, -3 and -9 in the rabbit cornea, and MMP-2, -9 in the rat cornea.17,18 The expression of MMP-2 and -9 during skin keratinocyte and corneal epithelial cell migration has been the most thoroughly investigated, and it has been shown that their expression generally depends on the activity of MMP-14. MMP-14 (MT1-MMP) is constitutively anchored to the cell membrane; it activates other MMPs such as MMP-2, and also cleaves various types of ECM molecules including collagens, laminins, fibronectin as well as its ligands, the integrins.13 The latent forms of some cytokines are also cleaved and activated by MMP-14.19 Overexpression of MMP-14 protein was found to stimulate HT1080 human fibrosarcoma cell migration.20 In contrast, the attenuation of MMP-14 expression using siRNA method decreased fibroblast invasiveness,21 angiogenesis of human microvascular endothelial cells,22 and human skin keratinocyte migration.10 The latter effect was shown to result from lowering MMP-9 expression. Other studies have shown that EGF has a critical role in MMP-9 expression during keratinocyte tumorigenesis and migration.23,24 On the other hand, TGFβ modulates MMP-9 production through the Ras/MAPK pathway in transformed mouse keratinocytes and NFκB induces cell migration by binding to the MMP-9 promoter in human skin primary cultures.25,26 Enhanced levels of pro-MMP-9 and active MMP-9 have also been noted in scratched corneal epithelia of diabetic rats.27There is evidence that MMP-14 activates a number of intracellular signaling pathways including the MAPK family pathway, focal adhesion kinase (FAK), Src family, Rac and CD44, during cell migration and tumor invasion.19,20,28 In COS-7 cells, ERK activation is stimulated by overexpression of MMP-14 and is essential for cell migration.29 These observations all indicate that MMP-14 plays an important role in cell migration, not only by regulating the activity or expression of downstream MMPs but also by processing and activating migration-associated molecules such as integrins, ECMs and a variety of intracellular signaling pathays.30Cell migration during wound healing is a remarkably complex phenomenon. TGFβ is just one small component of the overall process of wound healing and yet it triggers a multitude of reactions needed for cell migration. It is important to know what kinds of molecules are expressed when cell migration is initiated, but it is equally important to investigate the roles of these molecules and how their expression is regulated. Despite the availability of some information about how MMPs and signaling molecules can influence each other, much remains to be discovered in this area. It will be especially important to clarify how MMP-14 influences other signaling pathways since its role in cell migration is not restricted to digesting ECM molecules but also includes direct or indirect activation of cellular signaling pathways. 相似文献
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Double fertilization, uniquely observed in plants, requires successful sperm cell delivery by the pollen tube to the female gametophyte, followed by migration, recognition and fusion of the two sperm cells with two female gametic cells. The female gametophyte not only regulates these steps but also controls the subsequent initiation of seed development. Previously, we reported that loss of LORELEI, which encodes a putative glycosylphosphatidylinositol (GPI)-anchored protein, in the female reproductive tissues causes a delay in initiation of seed development. From these studies, however, it was unclear if embryos derived from fertilization of lre-5 gametophytes continued to lag behind wild-type during seed development. Additionally, it was not determined if the delay in initiation of seed development had any lingering effects during seed germination. Finally, it was not known if loss of LORELEI function affects seedling development given that LORELEI is expressed in eight-day-old seedlings. Here, we showed that despite a delay in initiation, lre-5/lre-5 embryos recover, becoming equivalent to the developing wild-type embryos beginning at 72 hours after pollination. Additionally, lre-5/lre-5 seed germination, and seedling and root development are indistinguishable from wild-type indicating that loss of LORELEI is tolerated, at least under standard growth conditions, in vegetative tissues.Key words: LORELEI, glycosylphosphatidylinositol (GPI)-anchored protein, embryogenesis, DD45, seed germination, primary and lateral root growth, seedling developmentDouble fertilization is unique to flowering plants. Upon female gametophyte reception of a pollen tube, the egg and central cells of the female gametophyte fuse with the two released sperm cells to form zygote and endosperm, respectively and initiate seed development.1 The female gametophyte controls seed development by (1) repressing premature central cell or egg cell proliferation until double fertilization is completed,1–3 (2) supplying factors that mediate early stages of embryo and endosperm development1,4,5 and (3) regulating imprinting of genes required for seed development.1,6The molecular mechanisms underlying female gametophyte control of early seed development are poorly understood. Although much progress has been made in identifying genes and mechanisms by which the female gametophyte represses premature central cell or egg cell proliferation until double fertilization is completed and regulates imprinting of genes required for seed development,1,6 only a handful of female gametophyte-expressed genes that affect early embryo7,8 and endosperm9 development after fertilization have been characterized. This is particularly important given that a large number of female gametophyte-expressed genes likely regulate early seed development.5We recently reported on a mutant screen for plants with reduced fertility and identification of a mutant that contained a large number of undeveloped ovules and very few viable seeds.10 TAIL-PCR revealed that this mutant is a new allele of LORELEI(LRE) [At4g26466].10,11 Four lre alleles have been reported;11 so, this mutant was designated lre-5.10 The Arabidopsis LORELEI protein contains 165 amino acids and possesses sequence features indicative of a glycosylphosphatidylinositol (GPI)-anchor containing cell surface protein. GPI-anchors serve as an alternative to transmembrane domains for anchoring proteins in cell membranes and GPI-anchored proteins participate in many functions including cell-cell signaling.12 相似文献
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Root elongation occurs by the generation of new cells from meristematic tissue within the apical 1–2 mm region of root tips. Therefore penetration of the soil environment is carried out by newly synthesized plant tissue, whose cells are inherently vulnerable to invasion by pathogens. This conundrum, on its face, would seem to reflect an intolerable risk to the successful establishment of root systems needed for plant life. Yet root tip regions housing the meristematic tissues repeatedly have been found to be free of microbial infection and colonization. Even when spore germination, chemotaxis, and/or growth of pathogens are stimulated by signals from the root tip, the underlying root tissue can escape invasion. Recent insights into the functions of root border cells, and the regulation of their production by transient exposure to external signals, may shed light on long-standing observations.Key words: border cells, chemotaxis, zoospores, neutrophil extracellular traps (NETs)…The evidence suggests that there has evolved within plants, mechanisms for extremely rapid adjustment to changes in the soil environment. The logical conclusion is that plants can and do selectively manipulate the ecological balances within the rhizosphere to their own advantage.1“Sloughed root cap cells” that detach from the root tip were long presumed to be moribund tissue serving to lubricate passage of the elongating root.2 The discovery nearly a century ago that these cells from Zea mays L. and Pisum sativum L. can remain 100% viable for weeks after detachment into hydroponic culture did not alter this perception.3 In recent decades, studies have shown that the cells from root caps of most species are metabolically active and can survive even after detachment into the soil.4 Moreover, the cell populations express distinct patterns of gene expression reflecting tissue specialization and were therefore given the name root ‘border’ cells.5 Like ‘border towns’ that exist at the boundary of disparate countries and cultures, border cells are part of the plant and part of the soil, yet distinct from both.The soil is a dynamic environment whose pH, surface charge, water availability, texture and composition can range markedly on a large and small scale.1,6,7 The concept of a ‘microniche’ emphasizes that the biological requirements for a particular soil microorganism may be met within one site but not another site only a micron away.8 Thus, the rhizosphere—the region adjacent to root surfaces—can support much higher levels of microorganisms than bulk soil a few millimeters distant.9 This phenomenon is recognized to be driven by an increased availability of nutrients released from plants into the external environment.10 Less well recognized is the dynamic variation that occurs along the root surface, and its significance in patterns of disease development. As roots emerge and the new tissue differentiates progressively through stages from root cap, root apical meristem, elongation zone, and finally mature roots with lignified cell walls, the material released into the environment also changes.11–13 More than 90% of bulk carbon released from young roots of legumes is delivered by the root cap, a 1 mm zone at the apex.14 Some pathogens are attracted specifically to the root tip region, presumably in response to such exudates.15,16 For example, instantaneous swarming occurs when a cotton root is placed into a suspension of Pythium dissotocum zoospores (Sup. Fig. 1). This host-specific attraction is specific to the root tip region where border cells are present (Sup. Fig. 2). Border cells remain attractive to zoospores when removed from the root (Sup. Fig. 3). The nature of the attractant is not known, but its impact is localized and transient (Sup. Fig. 4).Newly generated tissue is highly susceptible to infection by pathogens, in general, so elongating root tips would be predicted to be vulnerable to invasion. And yet, root apices repeatedly have been found to escape infection and colonization.17–19 Recent discoveries about parallels between mammalian white blood cells and root border cells may provide new insight into this apparent conundrum.20 Neutrophils, a type of white blood cell, are produced in response to infection. Neutrophil extracellular traps (NETs) then attract and kill the invader through a process that requires extracellular DNA (exDNA) and an array of extracellular proteins.21,22 Border cell production, like that of neutrophils, also is induced in response to signals from pathogens and root tip resistance to infection requires exDNA and an array of extracellular proteins.20,23 Root tip specific chemotaxis, like that seen with Pythium zoospores, has been presumed to involve steps in a process of pathogen invasion.15,16 It may, instead, involve a process of extracellular trapping and killing by cells designed to protect root meristems from invasion, in a manner analogous to that which occurs in mammalian defense. If tests confirm this model, the mystery of how root tips escape infection by soilborne pathogens they attract could be resolved. 相似文献
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New insights into the functional roles of CrRLKs in the control of plant cell growth and development
Receptor-like kinases (RLKs) are a family of transmembrane proteins with a variable ligand-binding extracellular domain and a cytoplasmic kinase domain. In Arabidopsis, there are ∼600 RLKs believed to have diverse functions during plant growth, development and interactions with the environment. Based on the variable extracellular domain, RLKs can be classified into different subfamilies. The CrRLK subfamily contains 17 members in Arabidopsis and characterization of some of its members suggests a role for these proteins in the regulation of growth and reproduction. This review focuses on the roles of CrRLKs in the regulation of polarized growth with emphasis on the newly identified signal transduction pathways activated downstream of CrRLKs. A picture is emerging where CrRLKs are part of a conserved signal transduction cascade important for growth maintenance in different cell types.Key words: CrRLKs, FERONIA, RAC/ROP, ROS, polar growthThe ability of plants to perceive and process environmental and internal information into coordinated responses is crucial to their adaptability and survival in constantly changing environments. Most of signal perception occurs at the plasma membrane of cells where membrane-associated receptors receive signals to activate downstream signaling cascades that regulate growth and development. In plants and animals alike, receptor-like kinases (RLKs) mediate many of the signaling events at the cell surface and in the model plant Arabidopsis they comprise a monophyletic family with more than 600 members.1 RLKs are transmembrane proteins with a variable N-terminal extracellular domain and a Ser/Thr intracellular kinase domain. The diversity of their extracellular domains suggests involvement in the transduction of a wide range of signals and allows them to be classified into different sub-families.2 The CrRLK1L subfamily (from here on referred to as CrRLK) is named after the first member characterized in Catharanthus roseus cell cultures3 and contains 17 members in Arabidopsis.4 Several members of this family have now been implicated in growth regulatory processes.THESEUS1 (THE1) was identified through a suppressor screen of a cellulose-deficient mutant (prc1-1) which has a short hypocotyl phenotype.5 Loss of THE1 function resulted in reduced growth inhibition in the prc1-1 the1 double mutant. Interestingly, the the1 mutation itself has no effect in wild type background, thus leading to the suggestion that THE1 functions as a sensor of cell wall integrity in situations where the cell wall is weakened and organ elongation would be detrimental for the plant.4,5A second CrRLK, FERONIA (FER), was first implicated in the regulation of female control of fertility. In the female gametophyte FER is involved in sensing pollen tube arrival and promoting its rupture which is necessary for double fertilization to occur.6,7 FER is in fact involved in several processes depending on the tissue where it is expressed. In hypocotyls, FER is involved in the integration of ethylene and brassinosteroid (BR) signals to regulate hypocotyl elongation in the dark.8 Moreover, FER, THE1 and the closely related HERCULES1 (HERK1), were found to regulate cell elongation by interacting with BR signaling.9 More recently, roles for FER in the regulation of root hair development and fungal invasion have been established.10,11 The pollen-specific ANXUR1 (ANX1) and ANXUR2 (ANX2) are closely related to FER and act redundantly to maintain pollen tube growth integrity during its journey through the style and ensure against precocious pollen tube rupture before reaching the ovule.12,13Apparently with different biological roles, all the CrRLK members analyzed thus far have an effect on the growth of plant cells. The present review focuses on their role during cell growth with emphasis on polar cell growth and the downstream pathways activated by CrRLKs. 相似文献
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Cell motility is a highly coordinated multistep process. Uncovering the mechanism of myosin II (MYO2) activation responsible for the contractility underlying cell protrusion and retraction provides clues on how these complementary activities are coordinated. Several protein kinases have been shown to activate MYO2 by phosphorylating the associated myosin light chain (MLC). Recent work suggests that these MLC kinases are strategically localized to various cellular regions during cell migration in a polarized manner. This localization of the kinases together with their specificity in MLC phosphorylation, their distinct enzymatic properties and the distribution of the myosin isoforms generate the specific contractile activities that separately promote the cell protrusion or retraction essential for cell motility.Key words: myosin, MLCK, ROK, MRCK, phosphorylation, cell migrationCell movement is a fundamental activity underlying many important biological events ranging from embryological development to immunological responses in the adult. A typical cell movement cycle entails polarization, membrane protrusion, formation of new adhesions, cell body translocation and finally rear retraction.1 A precise temporal and spatial coordination of these separate steps that take place in different parts of the cell is important for rapid and efficient movement.2One major event during eukaryotic cell migration is the myosin II (MYO2)-mediated contraction that underlies cell protrusion, traction and retraction.1,3 An emerging theme from collective findings is that there are distinct myosin contractile modules responsible for the different functions which are separately regulated by local myosin regulatory light chain (MLC) kinases. These kinases contribute to contractile forces that connect adhesion, protrusion and actin organization.2 Unraveling the regulation of these contractile modules is therefore pivotal to a better understanding of the coordination mechanism.At the lamellipodium, the conventional calcium/calmodulin-dependent myosin light chain kinase (MLCK) has been shown to play an essential role in a Rac-dependent lamellipodial extension.4 Inhibition of calmodulin or MLCK activity by specific photoactivatable peptides in motile eosinophils effectively blocks lamellipodia extension and net movement.5 Furthermore, there is a strong correlation between activated MLCK and phosphorylated MLC within the lamellipodia of Ptk-2 cells as revealed by fluorescence resonance energy transfer (FRET) analysis.6 More recent studies showed MLCK to regulate the formation of focal complexes during lamellipodia extension.7,8 Functionally, MLCK is thought to play a critical role in the environment-sensing mechanism that serves to guide membrane protrusion. It mediates contraction that exerts tension on integrin-extracellular matrix (ECM) interaction, which, depending on the rigidity of the substratum, will lead to either stabilization of adhesion resulting in protrusion or destabilization of attachment seen as membrane ruffling on non-permissive surfaces.8,9As a Rho effector, Rho-associated kinase (ROK/ROCK/Rho-kinase) has been shown to regulate stress fibers and focal adhesion formation by activating myosin, an effect that can be blocked by the specific ROK inhibitor Y-27632.10,11 Myosin activation by ROK is the effect of two phosphorylation events: the direct phosphorylation on MLC and the inhibition of myosin phosphatase through phosphorylation of its associated myosin-binding subunit (MBS).11 Consistent with this notion of a localization-function relationship, ROK and MBS, which can interact simultaneously with activated RhoA,11 have been shown to colocalize on stress fibers.12,13 In migrating cells, Rho and ROK activities have been mostly associated with the regulation of tail retraction, as inhibition of their activities often results in trailing tails due to the loss of contractility specifically confined to the cell rear.14,15 Tail retraction requires high contractile forces to overcome the strong integrin-mediated adhesion established at the rear end, an event which coincides with the strategic accumulation of highly stable and contractile stress fibers that assemble at the posterior region of migrating cells.MRCK was previously shown to phosphorylate MLC and promote Cdc42-mediated cell protrusion.16 More recently, it was found to colocalize extensively with and regulate the dynamics of a specific actomyosin network located in the lamella and cell center, in a Cdc42-dependent manner but independent of MLCK and ROK.17 The lamellar actomyosin network physically overlaps with, but is biochemically distinct from the lamellipodial actin meshwork.9,18 The former network consists of an array of filaments assembled in an arrangement parallel to the leading edge, undergoing continuous retrograde flow across the lamella, with their disassembly occurring at the border of the cell body zone sitting in a deeper region.17–19 Retrograde flow of the lamellar network plays a significant role in cell migration as it is responsible for generating contractile forces that support sustained membrane protrusion and cell body advancement.17–19It is therefore conceivable that these three known MLC kinases are regulated by different signaling mechanisms at different locations and on different actomyosin contractile modules. The coordination of the various modules will ensure persistent directional migration (Figure 1). Phosphorylation of MLC by PAK and ZIP kinase has also been reported, but their exact roles in this event have yet to be determined.20,21 It is also noteworthy that individual kinases can work independently of each other, as amply shown by evidence from inhibitor treatments. This is particularly true for MRCK in the lamella, whose activity on lamellar actomyosin flow is not affected by ML7 and Y-27632, the inhibitors of MLCK and ROK respectively.17 These findings further indicate that although both ROK and MRCK have been shown to upregulate phosphorylated MLC levels by inhibiting the myosins phosphatases,11,22 they are likely to act as genuine MLC kinases themselves, without the need of MLCK as previously suggested.11Open in a separate windowFigure 1Upper panel depicts a model for the specific activation of the different MLC kinases at various locations in the cell. In response to upstream signals, MLC kinases MLCK, MRCK and ROK are activated and localized to different regions. In the case of MRCK and ROK, the interaction of the GTP-bound Rho GTPase binding domain will determine the specific action of the downstream kinase, resulting in actomyosin contractility at different locations. The coordination of these signalling events is crucial for directional cell migration. Lower panel shows a typical front-rear location for Myosin 2A and 2B in a migrating U2OS cell.In conjunction with their differences in localization, the three MLC kinases show apparent individual preferences and specificity towards the MYO2 isoforms that they associate with. The two major MYO2 isoforms MYO2A and 2B are known to have distinct intracellular distributions that are linked to their individual functions (Figure 1).23,24 In motile cells, MYO2A localization that is skewed towards the protruding cell front is consistent with it being the major myosin 2 component of the lamellar filaments regulated by MRCK as well as its regulation by MLCK in lamellipodial contraction.8,17,19 In contrast, the enrichment of MYO2B at retracting cell rear conforms well with the requirement of thick and stable stress fibers capable of causing tail contraction and prevention of protrusion under the control of Rho/ROK signaling.23,25 The selection for MYO2B filaments in the cell rear stems from their more contractile and stable nature compared with MYO2A, a consequence of their higher time-averaged association with actin.26,27 Conversely, the lower tension property of MYO2A filaments suggests that they are more dynamic in nature,26,27 a characteristic which fits well with the dynamic actomyosin activities at the leading edge and lamella that regulate protrusion.It deserves special mention that the three MLC kinases display subtle differences in their specificity towards MLC. While MLCK and MRCK phosphorylate only a single Ser19 site (monophosphorylation),18,28 ROK is able to act on both Thr18 and Ser19 residues causing diphosphorylation of MLC,29 MLCK only causes diphosphorylation when present at higher concentrations.30 By further increasing its actin-activated ATPase activity, diphosphorylation of MLC has been shown to induce a higher myosin activation and filament stability.30–32 The use of specific antibodies that can differentiate between the two populations of phosphorylated MLC has been instrumental in revealing their localization and correlation with the activity of the MLC kinases. The emerging picture from these experiments is that mono and diphosphorylated MLC exhibit distinct distributions in migrating cells, with the monophosphorylated MLC localized more towards the protrusive region, while the diphosphorylated form is more enriched at the posterior end.21,33 Taking into account their biochemical properties, the polarized distributions of these differentially phosphorylated MLC coincide functionally with the segregation of the MYO2 isoforms and their corresponding regulators. These findings provide further support for the existence of segregated contractile modules in migrating cell and their distinctive regulation.The mechanisms that determine the specific segregation of the contractile modules and their regulation are unclear. However, some clues have emerged from recent studies. It has been shown that the C-terminal coiled-coil region of MYO2B is important for determining its localization in cell rear25 and which requires Rho/ROK activity as their inhibition resulted in the loss of this specific localization.23 Correspondingly, the inhibition of MRCK activity resulted in the loss of lamella-localized MYO2A.17 These findings suggest that activation of MYO2 filaments by their upstream regulators is important for their functional segregation and maintenance. It is noteworthy that both ROK and MRCK have distinct regulatory domains including the pleckstrin homology domains which have been shown to be essential for their localization, a process which may involve myosin interaction and lipid-dependent targeting as has been respectively shown for ROK and MRCK.11,13,16 Further, the specificity of MRCK for lamellar actomyosin is believed to be largely determined by the two proteins it forms a complex with: the adaptor LRAP35a, and the MYO2-related MYO18A. Activation of MYO18A by MRCK, a process bridged by LRAP35a, is a crucial step which facilitates MRCK regulation on lamellar MYO2A.17The mechanisms responsible for segregating the contractile modules and their regulators may also comprise a pathway that parallels the microtubule-modulatory Par6/aPKC/GSK3β signalling pathway which regulates cellular polarization. This notion is supported by both Cdc42 and Rho being common upstream regulators of these two pathways.34 GTPase activation may determine the localized activities of the separate contractile modules and create an actomyosin-based asymmetry across the cell body, which together with the microtubule-based activities, result in the formation of a front-back axis important for directional movement. The involvement of MRCK in MTOC reorientation and nuclear translocation events,35 and our unpublished observation that LRAP35a has a GSK3β-dependent microtubule stabilizing function are supportive of a possible cross-talk between these two pathways.In conclusion, the complex regulation of contractility in cell migration emphasizes the importance of the localization, specificity and enzymatic properties of the different MLC kinases and myosin isoforms involved. The initial excitement and confusion caused by the emergence of the different MLC kinases are fading, being now overtaken by the curiosity about how they cooperate and are coordinated while promoting cell motility. 相似文献
13.
Hisashi Kato-Noguchi 《Plant signaling & behavior》2011,6(8):1207-1209
The chemical cross talk between rice and barnyardgrass which is one of the most noxious weeds in rice cultivation was investigated. Allelopathic activity of rice was increased by the presence of barnyardgrass seedlings or barnyardgrass root exudates. Rice allelochemical, momilactone B, concentration in rice seedlings and momilactone B secretion level from rice were also increased by the presence of barnyardgrass seedlings or barnyardgrass root exudates. As momilactone B possesses strong growth inhibitory activity and acts as an allelochemical, barnyardgrass-induced rice allelopathy may be due to the increased momilactone B secretion. These results suggest that rice may respond to the presence of neighboring barnyardgrass by sensing the chemical components in barnyardgrass root exudates and increase allelopathic activity by elevated production and secretion levels of momilactone B. Thus, rice allelopathy may be one of the inducible defense mechanisms by chemical-mediated plant interaction between rice and barnyardgrass and the induced-allelopathy may provide a competitive advantage for rice through suppression of the growth of barnyardgrass.Key words: allelopathy, Echinochloa, chemical interaction, induced-allelopathy, momilactone, Oryza sativaThe chemical cross talk between host and symbiotic or parasitic plants is an essential process for the development of physical connections in symbiosis and parasitism.1–3 Barnyardgrass is one of the most common and noxious weeds in rice paddy fields.4 Although barnyardgrass is adapted rice production system due to its similarity in growth habit, the reason why barnyardgrass so often invades into the rice paddy fields is unknown. There might be some special interactions between both plant species.Plants are able to accumulate phytoalexins around infection sites of pathogens soon after sensing elicitors of pathogen origin. This accumulation of phytoalexins can protect the plants from further pathogen infection.5,6 Plants are also able to activate defense mechanisms against attacking herbivores by sensing volatile compounds, such as methacrolein and methyl jasmonate, released by herbivore-attacked plant cells. The volatile-sensed plants increase the production of phenolics, alkaloids, terpenes and defense proteins, which reduce herbivory attacks.7,8 Therefore, plants are able to elevate the defense mechanisms against several biotic stress conditions by detection of various compounds.Allelopathy is the direct influence of organic chemicals released from plants on the growth and development of other plants.9–11 Allelochemicals are such organic chemicals involved in the allelopathy.12,13 Allelochemicals can provide a competitive advantage for host-plants through suppression of soil microorganism and inhibition of the growth of competing plant species because of their antibacterial, antifungal and growth inhibitory activities.3,14,15Rice has been extensively studied with respect to its allelopathy as part of a strategy for sustainable weed management, such as breeding allelopathic rice strains. A large number of rice varieties were found to inhibit the growth of several plant species when these rice varieties were grown together with these plants under the field or/and laboratory conditions.16–20 These findings suggest that rice may produce and release allelochemicals into the neighboring environments and may inhibit the growth of the neighboring plants by the allelochemicals.Potent allelochemical, momilactone B, was isolated from rice root exudates.21 Momilactone B inhibits the growth of typical rice weeds like barnyardgrass and Echinochloa colonum at concentrations greater than 1 µM and the toxicity of momilactone B to rice itself was very low.22 In addition, rice plants secrete momilactone B from the roots into the rhizosphere over their entire life cycle.22 The observations suggest rice allelopathy may be primarily dependant on the secretion levels of momilactone B from the rice seedlings.22,23Allelopathic activity of rice exhibited 5.3- to 6.3-fold increases when rice and barnyardgrass seedlings were grown together. Root exudates of barnyardgrass seedlings also increased allelopathic activity and momilactone B concentration in rice seedlings. The increasing the exudate concentration increased the allelopathic activity and momilactone B concentration in rice.24 Thus, the chemical components in barnyardgrass root exudates may affect gene expressions involved in momilactone B biosynthesis. However, effects of the barnyardgrass root exudates on the secretion level of mimilactone B from rice has not yet reported.Rice seedlings were incubated in the medium containing barnyardgrass root exudates for 10 d, and secretion level of momilactone B by rice was determined (Fig. 1). The root exudates increased the secretion level significantly at concentrations greater than 30 mg/L of barnyardgrass root exudates, and increasing the concentration increased the secretion level. At concentrations of 300 mg/L of the root exudates, the secretion level was 10-fold greater than that in control (0 mg of root exudate). There was no significant difference in the osmotic potential between the medium contained barnyardgrass root exudates and control medium (all about 10 mmol/kg), and pH value of the medium was maintained at 6.0 throughout the experiments.25 These results suggest that unknown chemical components in the barnyardgrass root exudates may induce the secretion of momilactone B from rice. As momilactone B possesses strong phytotoxic and allelopathic activities,21–23,25 the elevated production and secretion of momilactone B in rice may provide a competitive advantage for root establishment through local suppression of pathogens and inhibition of the growth of competing plant species including barnyardgrass. Thus, barnyardgrass-induced rice allelopathy may be caused by the chemical components in the barnyardgrass root exudates.Open in a separate windowFigure 1Effects of barnyardgrass root exudates on momilactone B secretion level in rice. Rice seedlings were incubated in the medium containing barnyardgrass root exudates for 10 d, and secretion level of momilactone B was determined as described by Kato-Noguchi.24 The experiment was repeated six times with three assays for each determination. Different letters show significant difference (p < 0.01) according to Tukey''s HSD test.Although mechanisms of the exudation are not well understood, it is suggested that plants are able to secrete a wide variety of compounds from root cells by plasmalemma-derived exudation, endoplasmic-derived exudation and proton-pumping mechanisms.3,15 Through the root exudation of compounds, plants are able to regulate the soil microbial community in their immediate vicinity, change the chemical and physical properties of the soil, and inhibit the growth of competing plant species.3,14,15 The present research suggests that rice may be aware of the presence of neighboring barnyardgrass by detection of certain key in barnyardgrass root exudates, and this sensorial function may trigger a signal cascade resulting in increasing rice allelopathy through increasing production of momilactone B and secretion of momilactone B into the rhizosphere. Therefore, rice allelopathy may potentially be an inducible defense mechanism by chemical-mediated plant interactions between rice and barnyardgrass. 相似文献
14.
Eloise Foo Kaori Yoneyama Cassandra Hugill Laura J. Quittenden James B. Reid 《Plant signaling & behavior》2013,8(3)
As the newest plant hormone, strigolactone research is undergoing an exciting expansion. In less than five years, roles for strigolactones have been defined in shoot branching, secondary growth, root growth and nodulation, to add to the growing understanding of their role in arbuscular mycorrhizae and parasitic weed interactions.1 Strigolactones are particularly fascinating as signaling molecules as they can act both inside the plant as an endogenous hormone and in the soil as a rhizosphere signal.2-4 Our recent research has highlighted such a dual role for strigolactones, potentially acting as both an endogenous and exogenous signal for arbuscular mycorrhizal development.5 There is also significant interest in examining strigolactones as putative regulators of responses to environmental stimuli, especially the response to nutrient availability, given the strong regulation of strigolactone production by nitrate and phosphate observed in many species.5,6 In particular, the potential for strigolactones to mediate the ecologically important response of mycorrhizal colonization to phosphate has been widely discussed. However, using a mutant approach we found that strigolactones are not essential for phosphate regulation of mycorrhizal colonization or nodulation.5 This is consistent with the relatively mild impairment of phosphate control of seedling root growth observed in Arabidopsis strigolactone mutants.7 This contrasts with the major role for strigolactones in phosphate control of shoot branching of rice and Arabidopsis8,9 and indicates that the integration of strigolactones into our understanding of nutrient response will be complex. New data presented here, along with the recent discovery of phosphate specific CLE peptides,10 indicates a potential role for PsNARK, a component of the autoregulation of nodulation pathway, in phosphate control of nodulation. 相似文献
15.
Strigolactones' ability to regulate root development may be executed by induction of the ethylene pathway 总被引:1,自引:0,他引:1
Hinanit Koltai 《Plant signaling & behavior》2011,6(7):1004-1005
The newly defined phytohormones strigolactones (SLs) were recently shown to act as regulators of root development. Their positive effect on root-hair (RH) elongation enabled examination of their cross talk with auxin and ethylene. Analysis of wild-type plants and hormone-signaling mutants combined with hormonal treatments suggested that SLs and ethylene regulate RH elongation via a common regulatory pathway, in which ethylene is epistatic to SLs. The SL and auxin hormonal pathways were suggested to converge for regulation of RH elongation; this convergence was suggested to be mediated via the ethylene pathway, and to include regulation of auxin transport.Key words: strigolactone, auxin, ethylene, root, root hair, lateral rootStrigolactones (SLs) are newly identified phytohormones that act as long-distance shoot-branching inhibitors (reviewed in ref. 1). In Arabidopsis, SLs have been shown to be regulators of root development and architecture, by modulating primary root elongation and lateral root formation.2,3 In addition, they were shown to have a positive effect on root-hair (RH) elongation.2 All of these effects are mediated via the MAX2 F-box.2,3In addition to SLs, two other plant hormones, auxin and ethylene, have been shown to affect root development, including lateral root formation and RH elongation.4–6 Since all three phytohormones (SLs, auxin and ethylene) were shown to have a positive effect on RH elongation, we examined the epistatic relations between them by examining RH length.7 Our results led to the conclusion that SLs and ethylene are in the same pathway regulating RH elongation, where ethylene may be epistatic to SLs.7 Moreover, auxin signaling was shown to be needed to some extent for the RH response to SLs: the auxin-insensitive mutant tir1-1,8 was less sensitive to SLs than the wild type under low SL concentrations.7On the one hand, ethylene has been shown to induce the auxin response,9–12 auxin synthesis in the root apex,11,12 and acropetal and basipetal auxin transport in the root.4,13 On the other, ethylene has been shown to be epistatic to SLs in the SL-induced RH-elongation response.7 Therefore, it might be that at least for RH elongation, SLs are in direct cross talk with ethylene, whereas the cross talk between SL and auxin pathways may converge through that of ethylene.7 The reduced response to SLs in tir1-1 may be derived from its reduced ethylene sensitivity;7,14 this is in line with the notion of the ethylene pathway being a mediator in the cross talk between the SL and auxin pathways.The suggested ethylene-mediated convergence of auxin and SLs may be extended also to lateral root formation, and may involve regulation of auxin transport. In the root, SLs have been suggested to affect auxin efflux,3,15 whereas ethylene has been shown to have a positive effect on auxin transport.4,13 Hence, it might be that in the root, the SLs'' effect on auxin flux is mediated, at least in part, via the ethylene pathway. Ethylene''s ability to increase auxin transport in roots was associated with its negative effect on lateral root formation: ethylene was suggested to enhance polar IAA transport, leading to alterations in the quantity of auxin that unloads into the tissues to drive lateral root formation.4 Under conditions of sufficient phosphate, SL''s effect was similar to that of ethylene: SLs reduced the appearance of lateral roots; this was explained by their ability to change auxin flux.3 Taken together, one possibility is that the SLs'' ability to affect auxin flux and thereby lateral root formation in the roots is mediated by induction of ethylene synthesis.To conclude, root development may be regulated by a network of auxin, SL and ethylene cross talk.7 The possibility that similar networks exist elsewhere in the SLs'' regulation of plant development, including shoot architecture, cannot be excluded. 相似文献
16.
17.
Peptide signaling regulates a variety of developmental processes and environmental responses in plants.1–6 For example, the peptide systemin induces the systemic defense response in tomato7 and defensins are small cysteine-rich proteins that are involved in the innate immune system of plants.8,9 The CLAVATA3 peptide regulates meristem size10 and the SCR peptide is the pollen self-incompatibility recognition factor in the Brassicaceae.11,12 LURE peptides produced by synergid cells attract pollen tubes to the embryo sac.9 RALFs are a recently discovered family of plant peptides that play a role in plant cell growth.Key words: peptide, growth factor, alkalinization 相似文献
18.
Mitogen-activated protein kinase (MAPK) pathways play crucial roles in developmental and adaptive responses. Depending on the stimulus, MAPK activation regulates a wide variety of plant cell responses, such as proliferation, differentiation and cell death, which normally require precise spatial and temporal control. In this context, protein phosphatases play important roles by regulating the duration and magnitude of MAPK activities. During infection by non-host and incompatible host microorganisms, MAPK activity can promote a local cell death mechanism called hypersensitive response (HR), which is part of the plant defence response. HR-like responses require sustained MAPK activity and correlate with oxidative burst. We recently showed that MAPK phosphatase MKP2 positively controls biotic and abiotic stress responses in Arabidopsis. MKP2 interacts with MPK6 in HR-like responses triggered by fungal elicitors, suggesting that MKP2 protein is part of the mechanism involved in MAPK regulation during HR. Here we discuss the interplay of MAPK and MKP2 phosphatase signaling during cell death responses elicited by host-pathogen interactions.Key words: Arabidopsis, hypersensitive response (HR), MAPK, MPK6, MKP2, ROSDifferent studies have identified conserved components of MAPK pathways in plants and have provided evidence that MAPK signaling regulates a wide variety of plant biological responses.1 For example, MAPK signaling is required for the regulation of stomatal functions,2–4 hormone signaling5,6 and innate immunity responses.7–9 An increasing number of reports indicate that plant MAPKs, in particular tobacco SIPK/Ntf4 and WIPK and their Arabidopsis orthologs, MPK6 and MPK3, are converging points for signals elicited by different pathogens and play regulatory roles in disease responses.10One of the most efficient and immediate immune responses dependent on MAPK signaling is a mechanism of cell death called hypersensitive response (HR). HR is a rapid, localized cell death process at the site of pathogen infection, which is associated with specific molecular effects such as the generation of reactive oxygen species (ROS) and protein phosphorylation.11 The best evidence implicating MAPK activity in HR comes from gain-of-function studies overexpressing SIPK/Ntf4 and WIPK in tobacco leaves. In these experiments, activation of SIPK/Ntf4 kinases efficiently induces HR-like cell death,12,13 but the absence of endogenous WIPK function causes delayed induction of this HR phenotype, suggesting that WIPK activity facilitates or potentiates the SIPK signal.14 Similarly, overexpression analyses of Arabidopsis MPK3 and MPK6 proteins, either alone or co-expressed with activated upstream regulators (MKK proteins), also triggers a cell death phenotype,15 suggesting a coordinated role of MKK/MAPK signaling modules in HR.15 Thus, the involvement of MAPK activities such as SIPK/MPK6 in HR cell death responses is supported by different studies; however their regulation by phosphatases remains less understood.The main regulators of MAPKs are specific phosphatases belonging to various families, including PP2C Ser/Thr phosphatases, Tyr phosphatases (PTPs) or dual specificity phosphatases (DSPs) such as the MAPK phosphatase (MKP) subgroup.16,17 In general, dephosphorylation of MAPKs inactivates their function in many metabolic, developmental or adaptive responses. In the context of HR, we have recently shown that Arabidopsis MKP phosphatase MKP2 interacts with MPK6 in the response triggered by fungal elicitors. In particular, co-expression of MPK6 and MKP2 proteins in infected tobacco leaves significantly attenuates the cell death phenotype produced by expressing MPK6 alone, suggesting that MKP2 negatively regulates MAPK activities in this process.18 相似文献
19.
20.