Advertisement

Mitogen-Activated Protein Kinases and Wound Stress

  • Shigemi Seo
  • Yuko Ohashi
Part of the Results and Problems in Cell Differentiation book series (RESULTS, volume 27)

Summary

One of the most severe environmental stresses that plants encounter during their life cycle is wounding. Plants respond to wound stress by activating a set of genes that encode proteins involved in healing injured tissues. In recent years, mitogen-activated protein kinases have been implicated to be key signal molecules in the initial signal transduction pathways that mediate this stress to expression of genes.

Keywords

Salicylic Acid Jasmonic Acid Wound Response Wound Stress Plant Signal Transduction 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Albrecht T, Kehlen A, Stahl K, Knöfel H-D, Sembdner G, Weiler EW (1993) Quantification of rapid, transient increases in jasmonic acid in wounded plants using a monoclonal antibody. Planta 191 : 86–94CrossRefGoogle Scholar
  2. Bergey DR, Howe GA, Ryan CA (1996) Polypeptide signaling for plant defensive genes exhibits analogies to defense signaling in animals. Proc Natl Acad Sci USA 93: 12053–12058PubMedCrossRefGoogle Scholar
  3. Blumer KJ, Johnson GL (1994) Diversity in function and regulation of MAP kinase pathways. Trends Biochem Sci 19:236–240PubMedCrossRefGoogle Scholar
  4. Bögre L, Ligterink W, Meskiene I, Barker PJ, Heberle-Bors E, Huskisson NS, Hirt H (1997) Wounding induces the rapid and transient activation of a specific MAP kinase pathway. Plant Cell 9 : 75–83PubMedGoogle Scholar
  5. Brederode FTh, Linthorst HIM, Bol JF (1991) Differential induction of acquired resistance and PR gene expression in tobacco by virus infection, ethephone treatment, UV light and wounding. Plant Mol Biol 17:1117–1125Google Scholar
  6. Cano E, Mahadevan LC (1995) Parallel signal processing among mammalian MAPKs. Trends Biochem Sci 20 :117–122PubMedCrossRefGoogle Scholar
  7. Chandra S, Low PS (1995) Role of phosphorylation in elicitation of the oxidative burst in cultured soybean cells. Proc Natl Acad Sci USA 92 : 4120–4123PubMedCrossRefGoogle Scholar
  8. Cobb MH, Goldsmith EJ (1995) How MAP kinases are regulated. J Biol Chem 270 : 14843–14846PubMedCrossRefGoogle Scholar
  9. Creelman RA, Tierney ML, Mullet JE (1992) Jasmonic acid/methyl jasmonate accumulate in wounded soybean hypocotyls and modulate wound gene expression. Proc Natl Acad Sci USA 89 : 4938–4941PubMedCrossRefGoogle Scholar
  10. Davis RJ (1994) MAPKs: new INK exnands the group. Trends Biochem Sci 19 : 470–473PubMedCrossRefGoogle Scholar
  11. Dietrich A, Mayer JE, Hahlbrock K (1990) Fungal elicitor triggers rapid, transient, and specific protein phosphorylation in parsley cell suspension cultures. J Biol Chem 265 : 6360–6368PubMedGoogle Scholar
  12. Doares SH, Narvez-Vsquez J, Conconi A, Ryan CA (1995) Salicylic acid inhibits synthesis of proteinase inhibitors in tomato leaves induced by systemin and jasmonic acid. Plant Physiol 108:1741–1746PubMedGoogle Scholar
  13. Doi K, Gartner A, Ammerer G, Errede B, Shinkawa H, Sugimoto K, Matsumoto K (1994) MSG5, a novel protein phosphatase promotes adaptation to pheromone response in S. cerevisiae. EMBO J 13 : 61–70PubMedGoogle Scholar
  14. Duerr B, Gawienowski M, Ropp T, Jacobs T (1993) MsERK1: a mitogen-activated protein kinase from a flowering plant. Plant Cell 5 : 87–96PubMedGoogle Scholar
  15. Farmer EE, Ryan CA (1992) Octadecanoid precursors of jasmonic acid activate the synthesis of wound-inducible proteinase inhibitors. Plant Cell 4 : 129–134PubMedGoogle Scholar
  16. Farmer EE, Pearce G, Ryan CA (1989) In vitro phosphorylation of plant plasma membrane proteins in response to the proteinase inhibitor inducing factor. Proc Natl Acad Sci USA 86: 1539–1542PubMedCrossRefGoogle Scholar
  17. Farmer EE, Moloshok TD, Saxton MJ, Ryan CA (1991) Oligosaccharide signaling in plants. Specificity of oligouronide-enhanced plasma membrane protein phosphorylation. J Biol Chem 266:3140–3145PubMedGoogle Scholar
  18. Felix G, Grosskopf DG, Regenass M, Boller T (1991) Rapid changes of protein phosphorylation are involved in transduction of the elicitor signal in plant cells. Proc Natl Acad Sci USA 88: 8831–8834PubMedCrossRefGoogle Scholar
  19. Hemerly AS, Ferreira P, Engler J de A, Van Montagu M, Engler G, Inzé D (1993) cdc2a expression in Arabidopsis is linked with competence for cell division. Plant Cell 5 : 1711–1723PubMedGoogle Scholar
  20. Herskowitz I (1995) MAP kinase pathways in yeast: for mating and more. Cell 80 : 187–197PubMedCrossRefGoogle Scholar
  21. Hirt H (1997) Multiple roles of MAP kinases in plant signal transduction. Trends Plant Sci 2: 11–15CrossRefGoogle Scholar
  22. Jonak C, Heberle-Bors E, Hirt H (1994) MAP kinases: universal multi-purpose signaling tools. Plant Mol Biol 24 : 407–416PubMedCrossRefGoogle Scholar
  23. Jonak C, Kiegerl S, Lloyd C, Chan J, Hirt H (1995) MMK2, a novel alfalfa MAP kinase, specifically complements the yeast MPK1 function. Mol Gen Genet 248 : 686–694PubMedCrossRefGoogle Scholar
  24. Jonak C, Kiegerl S, Ligterink W, Barker PJ, Huskisson NS, Hirt H (1996) Stress signaling in plants: a mitogen-activated protein kinase pathway is activated by cold and drought. Proc Natl Acad Sci USA 93 : 11274–11279PubMedCrossRefGoogle Scholar
  25. Koiwa H, Bressan RA, Hasegawa PM (1997) Regulation of protease inhibitors and plant defense. Trends Plant Sci 2 : 379–384CrossRefGoogle Scholar
  26. Lawton MA, Lamb CJ (1987) Transcriptional activation of plant defense genes by fungal elicitor, wounding, and infection. Mol Cell Biol 7: 335–341PubMedGoogle Scholar
  27. Ligterink W, Kroj T, Zur Nieden U, Hirt H, Scheel D (1997) Receptor-mediated activation of a MAP kinase in pathogen defense of plants. Scince 276 : 2054–2057CrossRefGoogle Scholar
  28. Machida Y, Nishihama R, Kitakura S (1997) Progress in studies of plant homologs of mitogenactivated protein (MAP) kinase and potential upstream components in kinase cascades. Crit Rev Plant Sci 16 : 481–496Google Scholar
  29. MacKintosh C, Lyon GD, MacKintosh RW (1994) Protein phosphatase inhibitors activate antifungal defence responses of soybean cotyledons and cell cultures. Plant J 5 :137–147CrossRefGoogle Scholar
  30. Malamy J, Carr JP, Klessig DF, Raskin I (1990) Salicylic acid: a likely endogenous signal in the resistance response of tobacco to viral infection. Science 250 :1002–1004PubMedCrossRefGoogle Scholar
  31. Malone M (1992) Kinetics of wound-induced hydraulic signals and variation potentials in wheat seedlings. Planta 187 : 505–510CrossRefGoogle Scholar
  32. Memelink J, Linthorst HJM, Schilperoort RA, Hoge JHC (1990) Tobacco genes encoding acidic and basic isoforms of pathogenesis-related proteins display different expression patterns. Plant Mol Biol 14: 119–126PubMedCrossRefGoogle Scholar
  33. Meskiene I, Bögre L, Glaser W, Balog J, Brandstötter M, Zwerger K, Ammerer G, Hirt H (1998) MP2C, a plant protein phosphatase 2C, functions as a negative regulator of mitogen-activated protein kinase pathways in yeast and plants. Proc Natl Acad Sci USA 95 : 1938–1943PubMedCrossRefGoogle Scholar
  34. Mizoguchi T, Irie K, Hirayama T, Hayashida N, Yamaguchi-Shinozaki K, Matsumoto K, Shinozaki K (1996) A gene encoding a mitogen-activated protein kinase kinase kinase is induced simultaneously with genes for a mitogen-activated protein kinase and an S6 ribosomal protein kinase by touch, cold, and water stress in Arabidopsis thaliana. Proc Natl Acad Sci USA 93: 765–769PubMedCrossRefGoogle Scholar
  35. Mizoguchi T, Ichimura K, Shinozaki K (1997) Environmental stress response in plants: the role of mitogen-activated protein kinases. Trends Biotechnol 15 : 15–19PubMedCrossRefGoogle Scholar
  36. Niki T, Mitsuhara I, Seo S, Ohtsubo N, Ohashi Y (1998) Antagonistic effect of salicylic acid and jasmonic acid on the expression of pathogenesis-related (PR) protein genes in wounded mature tobacco leaves. Plant Cell Physiol 39 : 500–507CrossRefGoogle Scholar
  37. Nishida E, Gotoh Y (1993) The MAP kinase cascade is essential for diverse signal transduction pathways. Trends Biochem Sci 18: 128–131PubMedCrossRefGoogle Scholar
  38. Nishihama R, Banno H, Shibata W, Hirano K, Nakashima M, Usami S, Machida Y (1995) Plant homologues of components of MAPK (mitogen-activated protein kinase) signal pathways in yeast and animal cells. Plant Cell Physiol 36 : 749–757PubMedGoogle Scholar
  39. O’Donnell PJ, Calvert C, Atzorn Z, Wasternack C, Leyser HMO, Bowles DJ (1996) Ethylene as a signal mediating the wound response of tomato plants. Science 274: 1914–1917PubMedCrossRefGoogle Scholar
  40. Pelech SL, Sanghera JS (1992) Mitogen-activated protein kinases: versatile transducers for cell signaling. Trends Biochem Sci 17 : 233–238PubMedCrossRefGoogle Scholar
  41. Peña-Cortés H, Albrecht T, Prat S, Weiler EW, Willmitzer L (1993) Aspirin prevents wound-induced gene expression in tomato leaves by blocking jasmonic acid biosynthesis. Planta 191: 123–128CrossRefGoogle Scholar
  42. Peña-Cortés H, Fisahn J, Willmitzer L (1995) Signals involved in wound-induced proteinase inhibitor II gene expression in tomato and potato plants. Proc Natl Acad Sci USA 92 : 4106–4113PubMedCrossRefGoogle Scholar
  43. Redhead CR, Palme K (1996) The genes of plant signal transduction. Crit Rev Plant Sci 15: 425–454Google Scholar
  44. Reinbothe S, Mollenhauer B, Reinbothe C (1994) JIPs and RIPs: the regulation of plant gene expression by jasmonates in response to environmental cues and pathogens. Plant Cell 6: 1197–1209PubMedGoogle Scholar
  45. Ryan CA (1990) Proteinase inhibitors in plants: genes for improving defenses against insects and pathogens. Annu Rev Phytopathol 28 : 425–449CrossRefGoogle Scholar
  46. Sano H, Seo S, Koizumi N, Niki T, Iwamura H, Ohashi Y (1996) Regulation of cytokinin of endogenous levels of jasmonic and salicylic acids in mechanically wounded tobacco plants. Plant Cell Physiol 37 : 762–769CrossRefGoogle Scholar
  47. Seo S, Okamoto M, Seto H, Ishizuka K, Sano H, Ohashi Y (1995) Tobacco MAP kinase: a possible mediator in wound signal transduction pathways. Science 270: 1988–1992PubMedCrossRefGoogle Scholar
  48. Seo S, Sano H, Ohashi Y (1997) Jasmonic acid in wound signal transduction pathways. Physiol Plant 101 : 740–745CrossRefGoogle Scholar
  49. Seo S, Sano H, Ohashi Y (1999) Jasmonate-based wound signal transduction requires activation of WIPK. a mitogen-activated protein kinase. Plant Cell 11 289–298Google Scholar
  50. Shiozaki K, Russell P (1995) Counteractive roles of protein phosphatase 2C (PP2C) and a MAP kinase kinase homolog in the osmoregulation of fission yeast. EMBO J 14 : 492–502PubMedGoogle Scholar
  51. Staswick PE (1992) Jasmonate, genes, and fragrant signals. Plant Physiol 99 : 804–807PubMedCrossRefGoogle Scholar
  52. Stone JM, Walker JC (1995) Plant protein kinase families and signal transduction. Plant Physiol 108 : 451–457PubMedCrossRefGoogle Scholar
  53. Stratmann JW, Ryan CA (1997) Myeline basic protein kinase activity in tomato leaves is induced systemically by wounding and increases in response to systemin and oligosaccharide elicitors. Proc Natl Acad Sci USA 94 : 11085–11089PubMedCrossRefGoogle Scholar
  54. Sun H, Charles CH, Lau LF, Tonks NK (1993) MKP-1 (3CH134), an immediate early gene product, is a dual specificity phosphatase that dephosphorylates MAP kinase in vivo. Cell 75: 487–493PubMedCrossRefGoogle Scholar
  55. Suzuki K, Shinshi H (1996) Protein kinases in elicitor signal transduction in plant cells. J Plant Res 109 : 253–263CrossRefGoogle Scholar
  56. Usami S, Banno H, Ito Y, Nishihama R, Machida Y (1995) Cutting activates a 46-kDa protein kinase in plants. Proc Natl Acad Sci USA 92 : 8660–8664PubMedCrossRefGoogle Scholar
  57. Wasternack C, Parthier B (1997) Jasmonate-signalled plant gene expression. Trends Plant Sci 2: 302–307CrossRefGoogle Scholar
  58. Wildon DC, Thain JF, Minchin PEH, Gubb IR, Reilly AJ, Skipper YD, Doherty HM, O’Donnell PJ, Bowles DJ (1992) Electrical signalling and systemic proteinase inhibitor induction in the wounded plant. Nature 360 : 62–65CrossRefGoogle Scholar
  59. Wilson C, Eller N, Gartner A, Vicente O, Heberle-Bors E (1993) Isolation and characterization of a tobacco cDNA clone encoding a putative MAP kinase. Plant Mol Biol 23 : 543–551PubMedCrossRefGoogle Scholar
  60. Wilson C, Anglmayer R, Vicente O, Heberle-Bors E (1995) Molecular cloning. functional expression in Escherichia col, and characterization of multiple mitogen-activated protein kinases from tobacco. Eur T Biochem 233 : 249–257CrossRefGoogle Scholar
  61. Wilson C, Voronin V, Touraev A, Vicente O, Heberle-Bors E (1997) A developmentally regulated MAP kinase activated by hydration in tobacco pollen. Plant Cell 9 : 2093–2100PubMedGoogle Scholar
  62. Wurgler-Murphy SM, Maeda T, Witten EA, Saito H (1997) Regulation of the Saccharomyces cerevisiae HOGl mitogen-activated protein kinase by the PTP2 and PTP3 protein tyrosine phosphatases. Mol Cell Biol 17: 1289–1297PubMedGoogle Scholar
  63. Zhang S, Klessig DF (1997) Salicylic acid activates a 48-kDa MAP kinase in tobacco. Plant Cell 9: 809–824PubMedGoogle Scholar
  64. Zhang S, Klessig DF (1998) The tobacco wounding -activated protein kinase is encoded by SIPK. Proc Natl Acad Sci USA 95 : 7225–7230PubMedCrossRefGoogle Scholar
  65. Zhang S, Du H, Klessig DF (1998) Activation of the tobacco SIP kinase by both a cell wall-derived carbohydrate elicitor and purified proteinaceous elicitins from Phytophthora spp. Plant Cell 10 : 435–449PubMedGoogle Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 2000

Authors and Affiliations

  • Shigemi Seo
  • Yuko Ohashi
    • 1
  1. 1.Department of Molecular GeneticsNational Institute of Agrobiological ResourcesTsukuba, IbarakiJapan

Personalised recommendations