Plant Homologues of Components of MAPK (Mitogen-Activated Protein Kinase) Signal Pathways in Yeast and Animal Cells

Nishihama, Ryuichi; Banno, Hiroharu; Shibata, Wataru; Hirano, Kazumi; Nakashima, Marina; Usami, Shoji; Machida, Yasunori

doi:10.1093/oxfordjournals.pcp.a078818

Cited by 60 publications

(39 citation statements)

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“…It has been proposed that the initial wound signal stimulates the phosphorylation of protein kinases and activates enzymes involved in jasmonate synthesis . This hypothesis was partly substantiated by our finding that a rapid, systemic increase in transcripts encoding WIPK, a mitogen-activated protein (MAP) kinase homolog in tobacco, was observed in response to mechanical wounding (Seo et al, 1995).MAP kinases constitute a family of serine/threonine protein kinases that have been well conserved in all eukaryotes throughout evolution (Nishida and Gotoh, 1993;Jonak et al, 1994;Nishihama et al, 1995). They are enzymatically activated when threonine and tyrosine residues within the TXY motif in subdomain VIII are phosphorylated (Anderson et al, 1990).…”

mentioning

confidence: 86%

“…MAP kinases constitute a family of serine/threonine protein kinases that have been well conserved in all eukaryotes throughout evolution (Nishida and Gotoh, 1993;Jonak et al, 1994;Nishihama et al, 1995). They are enzymatically activated when threonine and tyrosine residues within the TXY motif in subdomain VIII are phosphorylated (Anderson et al, 1990).…”

Section: Introductionmentioning

confidence: 99%

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Jasmonate-Based Wound Signal Transduction Requires Activation of WIPK, a Tobacco Mitogen-Activated Protein Kinase

1999

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A gene encoding a tobacco mitogen-activated protein kinase (WIPK) is transcriptionally activated in response to wounding. Transgenic tobacco plants, in which expression of endogenous wipk was suppressed, did not accumulate jasmonic acid or its methyl ester when wounded, suggesting that WIPK is involved in jasmonate-mediated wound signal transduction. Here, we demonstrate that activation of WIPK is required for triggering the jasmonate-mediated signal transduction cascade that occurs when wild-type tobacco plants are wounded. We also show that when plants are wounded, WIPK is rapidly and transiently activated, whereas the quantity of WIPK protein is maintained at a constant level. A transgenic tobacco plant in which the wipk gene was constitutively expressed at a high level showed constitutive enzymatic activation of WIPK and exhibited three-to fourfold higher levels of jasmonate than did its wild-type counterpart. This plant also showed constitutive accumulation of jasmonate-inducible proteinase inhibitor II transcripts. These results show that WIPK is activated in response to wounding, which subsequently causes an increase in jasmonate synthesis. INTRODUCTIONPlants quickly respond to wound stress, such as physical injury and insect attack, by activating diverse genes that encode proteins involved in healing injured tissues. Representative examples are the proteinase inhibitors (Ryan, 1990) whose genes are transcriptionally activated by jasmonic acid (JA) or its methyl ester (MeJA) Peña-Cortés et al., 1992). Further studies have revealed that synthesis of proteinase inhibitors is stimulated not only by jasmonates but also by their biosynthetic precursors, linolenic, 13( S )-hydroperoxylinolenic, and 12-oxo-phytodienoic acids . These studies suggest that plant wound signaling is mediated by octadecanoid pathways, which are analogous to inflammation signaling pathways in animals (Bergey et al., 1996). Jasmonates have been shown to accumulate in the plant body upon mechanical wounding (Albrecht et al., 1992;Creelman et al., 1992), a further indication that they are natural inducers of proteinase inhibitors. It has been proposed that the initial wound signal stimulates the phosphorylation of protein kinases and activates enzymes involved in jasmonate synthesis . This hypothesis was partly substantiated by our finding that a rapid, systemic increase in transcripts encoding WIPK, a mitogen-activated protein (MAP) kinase homolog in tobacco, was observed in response to mechanical wounding (Seo et al., 1995).MAP kinases constitute a family of serine/threonine protein kinases that have been well conserved in all eukaryotes throughout evolution (Nishida and Gotoh, 1993;Jonak et al., 1994;Nishihama et al., 1995). They are enzymatically activated when threonine and tyrosine residues within the TXY motif in subdomain VIII are phosphorylated (Anderson et al., 1990). In animals and yeasts, MAP kinases function in the transduction of extracellular stimuli into intracellular signals to regulate expression of genes that are essent...

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mentioning

confidence: 86%

Section: Introductionmentioning

confidence: 99%

Jasmonate-Based Wound Signal Transduction Requires Activation of WIPK, a Tobacco Mitogen-Activated Protein Kinase

1999

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“…In plant and animal systems, growth signaling pathways and the cell cycle machinery appear to share many common factors (28,29). Nevertheless, given the immobile attributes of plant life and plant cells, which are surrounded by rigid cell walls (5), some aspects of plant growth and cell proliferation are likely to be regulated and coordinated in a different way from those of animals (19).…”

Section: Coordination Of Cell Proliferation and Growthmentioning

confidence: 99%

Plant organ size control: AINTEGUMENTA regulates growth and cell numbers during organogenesis

Mizukami

Fischer

2000

Proc. Natl. Acad. Sci. U.S.A.

759

700

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The control of cell proliferation during organogenesis plays an important role in initiation, growth, and acquisition of the intrinsic size of organs in higher plants. To understand the developmental mechanism that controls intrinsic organ size by regulating the number and extent of cell division during organogenesis, we examined the function of the Arabidopsis regulatory gene AINTEGUMENATA (ANT). Previous observations revealed that ANT regulates cell division in integuments during ovule development and is necessary for floral organ growth. Here we show that ANT controls plant organ cell number and organ size throughout shoot development. Loss of ANT function reduces the size of all lateral shoot organs by decreasing cell number. Conversely, gain of ANT function, via ectopic expression of a 35S::ANT transgene, enlarges embryonic and all shoot organs without altering superficial morphology by increasing cell number in both Arabidopsis and tobacco plants. This hyperplasia results from an extended period of cell proliferation and organ growth. Furthermore, cells ectopically expressing ANT in fully differentiated organs exhibit neoplastic activity by producing calli and adventitious roots and shoots. Based on these results, we propose that ANT regulates cell proliferation and organ growth by maintaining the meristematic competence of cells during organogenesis.A lthough plant growth is influenced greatly by external environmental factors, it appears that the intrinsic size of plant organs is determined by internal developmental factors. Evidence for intrinsic organ size control is seen by the remarkable uniformity of organ size among individuals within a species (e.g., Arabidopsis thaliana petal size) and by the conspicuous differences in organ size between related species (e.g., A. thaliana versus Brassica napus petal size). Previous genetic analysis has focused primarily on the role of polarized cell elongation in determining organ morphology (1, 2). However, disparity in size of a particular organ (e.g., petal) between species is primarily the result of differences in cell number, not cell size (3). Thus, the intrinsic organ size of a species is determined primarily by organ cell number. Population genetics has indicated that intrinsic plant organ size might be regulated by a polygenic system, and in some species quantitative trait loci that affect plant organ size have been studied (4). However, how intrinsic organ size is genetically controlled, or the nature of the developmental regulators involved in plant organ size control, is not well understood.The total cell number of an organ is determined by the number of divisions of undifferentiated stem cells [i.e., meristematic cells (5)]. During shoot development, lateral organs are initiated as primordia from apical and lateral meristems (6, 7). Although most cells in organ primordia are meristematic and proliferate, cells lose meristematic competence and withdraw from the cell cycle as organs develop. Thus, the maintenance of meristematic competence of cells is ...

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“…These include the p47 funga1 elicitor-activated kinase (Suzuki and Shinshi, 1995) and the p46 cutting-activated kinase (Usami et al, 1995). Because purification of either of these proteins has yet to be reported, they cannot be directly compared with the purified p48 SIP kinase.…”

Section: The P48 Sip Kinase 1s a Member Of The Map Kinase Familymentioning

confidence: 99%

“…These include the tobacco cutting (wounding)-activated p46 kinase (Se0 et al, 1995;Usami et al, 1995), the funga1 elicitor-activated p47 kinase from tobacco (Suzuki and Shinshi, 1995), and the abscisic acid-activated kinase from barley (Knetsch et al, 1996). In this study, we report the identification and characterization of a 48-kD kinase that is called SIP kinase (for SA-jnduced protein kinase).…”

Section: Introductionmentioning

confidence: 99%

Salicylic acid activates a 48-kD MAP kinase in tobacco.

1997

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The involvement of phosphorylalion/dephosphorylation in the salicylic acid (SA) signal transduction pathway leading t o pathogenesis-related gene induction has previously been demonstrated using kinase and phosphatase inhibitors. Here, we show that in tobacco suspension cells, SA induced a rapid and transient activation of a 48-kD kinase that uses myelin basic protein as a substrate. This kinase is called the p48 SIP kinase (for ZA-jnduced protein kinase). Biologically active analogs of SA, which induce pathogenesis-related genes and enhanced resistance,also activated this kinase, whereas inactive analogs did not. Phosphorylation of a tyrosine residue(s) in the SIP kinase was associated with its activation. The SIP kinase was purified to homogeneity from SA-treated tobacco suspension culture cells. The purified SIP kinase is strongly phosphorylated on a tyrosine residue(s), and treatment with either protein tyrosine or serine/threonine phosphatases abolished its activity. Using primers corresponding t o the sequences of interna1 tryptic peptides, we cloned the SIP kinase gene. Analysis of the SIP kinase sequence indicates that it belongs t o the MAP kinase family and that it is distinct from the other plant MAP kinases previously implicated in stress responses, suggesting that different members of the MAP kinase family are activated by different stresses.

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Plant Homologues of Components of MAPK (Mitogen-Activated Protein Kinase) Signal Pathways in Yeast and Animal Cells

Cited by 60 publications

References 0 publications

Jasmonate-Based Wound Signal Transduction Requires Activation of WIPK, a Tobacco Mitogen-Activated Protein Kinase

Jasmonate-Based Wound Signal Transduction Requires Activation of WIPK, a Tobacco Mitogen-Activated Protein Kinase

Plant organ size control: AINTEGUMENTA regulates growth and cell numbers during organogenesis

Salicylic acid activates a 48-kD MAP kinase in tobacco.

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