Plant Molecular Biology

, Volume 38, Issue 6, pp 919–927 | Cite as

Protein phosphatase 2C (PP2C) function in higher plants

  • Pedro L. Rodriguez


In the past few years, molecular cloning studies have revealed the primary structure of plant protein serine/threonine phosphatases. Two structurally distinct families, the PP1/PP2A family and the PP2C family, are present in plants as well as in animals. This review will focus on the plant PP2C family of protein phosphatases. Biochemical and molecular genetic studies in Arabidopsis have identified PP2C enzymes as key players in plant signal transduction processes. For instance, the ABI1/ABI2 PP2Cs are central components in abscisic acid (ABA) signal transduction. Arabidopsis mutants containing a single amino acid exchange in ABI1 or ABI2 show a reduced response to ABA. Another member of the PP2C family, kinase-associated protein phosphatase (KAPP), appears to be an important element in some receptor-like kinase (RLK) signalling pathways. Finally, an alfalfa PP2C acts as a negative regulator of a plant mitogen-activated protein kinase (MAPK) pathway. Thus, the plant PP2Cs function as regulators of various signal transduction pathways.


Abscisic Acid Protein Phosphatase Single Amino Acid Acid Exchange Molecular Genetic Study 
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.


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  1. 1.
    Becraft PW, Stinard PS, McCarty DR: CRINKL Y4: a TNFR like receptor kinase involved in maize epidermal differentiation. Science 273: 1406–1409 (1996).Google Scholar
  2. 2.
    Bertauche N, Leung J, Giraudat J: Protein phosphatase activity of abscisic acid insensitive1 (ABI1) protein from Arabidopsis thaliana. Eur J Biochem 241: 193–200 (1996).Google Scholar
  3. 3.
    Bleecker AB, Schaller GE: The mechanism of ethylene perception. Plant Physiol 111: 653–660 (1996).Google Scholar
  4. 4.
    Bork P, Brown NP, Hegyi H, Schultz J: The protein phosphatase 2C (PP2C) superfamily: detection of bacterial homologues. Protein Sci 5: 1421–1425 (1996).Google Scholar
  5. 5.
    Bögre L, Ligterink W, Meskiene I, Barker PJ, Heberle-Bors E, Huskisson NS, Hirt H: Wounding induces the rapid and transient activation of a specific MAP kinase pathway. Plant Cell 9: 75–83 (1997).Google Scholar
  6. 6.
    Braun DM, Stone JM, Walker JC: Interaction of the maize and Arabidopsis kinase interaction domains with a subset of receptor-like protein kinases: implications for transmembrane signaling in plants. Plant J 12: 83–95 (1997).Google Scholar
  7. 7.
    Bruxelles GL: Abscisic acid induces the alcohol dehydrogenase gene in Arabidopsis. Plant Physiol 111: 381–391 (1996).Google Scholar
  8. 8.
    Chandler PM, Robertson M: Gene expression regulated by abscisic acid and its relation to stress tolerance. Annu Rev Plant Physiol Plant Mol Biol 45: 113–141 (1994).Google Scholar
  9. 9.
    Chang C, Schaller GE, Patterson SE, Kwok SF, Meyerowitz EM, Bleecker AB: The TMK1 gene from Arabidopsis codes for a protein with structural and biochemical characteristics of a receptor protein kinase. Plant Cell 4: 1263–1271 (1992).Google Scholar
  10. 10.
    Chen MX, McPartlin AE, Brown L, Chen YH, Barker HM, Cohen PTW: A novel human protein serine/threonine phosphatase, which possesses four tetratricopeptide repeat motifs and localizes to the nucleus. EMBO J 13: 4278–4290 (1994).Google Scholar
  11. 11.
    Clark SE, Willians RW, Meyerowitz EM: The CLAVATA1 gene encodes a putative receptor kinase that controls shoot and floral meristem size in Aribidopsis. Cell 89: 575–585 (1997).Google Scholar
  12. 12.
    Cohen P, Cohen PTW: Protein phosphatases come of age. J Biol Chem 264: 21435–21438 (1989).Google Scholar
  13. 13.
    Cohen P: The structure and regulation of protein phosphatases. Annu Rev Biochem 58: 453–508 (1989).Google Scholar
  14. 14.
    Cohen PTW: Nomenclature and chromosomal localization of human protein serine/threonine phosphatase genes. Adv Prot Phos 8: 371–374 (1994).Google Scholar
  15. 15.
    Corton JM, Gillespie JG, Hardie DG: Role of the AMPactivated protein kinase in the cellular stress response. Curr Biol 4: 315–324 (1994).Google Scholar
  16. 16.
    Das AK, Helps NR, Cohen PTW, Barford D: Crystal structure of protein serine/threonine phosphatase 2C at 2.0 Å resolution. EMBO J 15: 6798–6809 (1996).Google Scholar
  17. 17.
    Duncan L, Alper S, Arigoni F, Losick R, Stragier P: Activation of cell-specific transcription by a serine phosphatase at the site of asymmetric division. Science 270: 641–644 (1995).Google Scholar
  18. 18.
    Fantl WJ, Johnson DE, Williams LT: Signaling by receptor tyrosine kinases. Annu Rev Biochem 62: 453–481 (1993).Google Scholar
  19. 19.
    Finkelstein RR, Somerville CR: Three classes of abscisic acid (ABA)-insensitive mutations of Arabidopsis define genes that control overlapping subsets of ABA responses. Plant Physiol 94: 1172–1179 (1990).Google Scholar
  20. 20.
    Gaits F, Shiozaki K, Russel P: Protein phosphatase 2C acts independently of stress-activated kinase cascade to regulate the stress response in fission yeast. J Biol Chem 272: 17873–17879 (1997).Google Scholar
  21. 21.
    Gilmour SJ, Thomashow MF: Cold acclimation and coldregulated gene expression in ABA mutants of Arabidopsis thaliana. Plant Mol Biol 17: 1233–1240 (1991).Google Scholar
  22. 22.
    Gosti F, Bertauche N, Vartanian N, Giraudat J: Abscisic aciddependent and-independent regulation of gene expression by progressive drought in Arabidopsis thaliana. Mol Gen Genet 246: 10–18 (1995).Google Scholar
  23. 23.
    Herbst R, Carroll PM, Allard JD, Schilling J, Raabe T, Simon MA: Daughter of Sevenless is a substrate of the phosphotyrosine phosphatase Corkscrew and functions during Sevenless signaling. Cell 85: 899–909 (1996).Google Scholar
  24. 24.
    Herskowitz I: Functional inactivation of genes by dominant negative mutations. Nature 329: 219–222 (1987).Google Scholar
  25. 25.
    Hubbard MJ, Cohen P: On target with a new mechanism for the regulation of protein phosphorylation. Trends Biochem Sci 18: 172–177 (1993).Google Scholar
  26. 26.
    Jonak C, Kiegerl S, Ligterink W, Barker PJ, Huskisson NS, Hirt H: Stress signaling in plants: a mitogen-activated protein kinase pathway is activated by cold and drought. Proc Natl Acad Sci USA 93: 11274–11279 (1996).Google Scholar
  27. 27.
    Klee CB, Draetta GF, Hubbard MJ: Calcineurin. Adv Enzymol 61: 149–200 (1988).Google Scholar
  28. 28.
    Koornneef M, Reuling G, Karssen CM: The isolation and characterization of abscisic acid-insensitive mutants of Arabidopsis thaliana. Physiol Plant 61: 377–383 (1984).Google Scholar
  29. 29.
    Kuromori T, Yamamoto M: Cloning of cDNAs from Arabidopsis thaliana that encode a putative protein phosphatase 2C and a human Dr1-like protein by transformation of a fission yeast mutant. Nucl Acids Res 22: 5296–5301 (1994).Google Scholar
  30. 30.
    Leube MP, Grill E, Amrhein N: ABI1 of Arabidopsis is a protein serine/threonine phosphatase highly regulated by proton and magnesium ion concentration. FEBS Lett 424: 96–100 (1998).Google Scholar
  31. 31.
    Leung J, Bouvier-Durand M, Morris P-C, Guerrier D, Chefdor F, Giraudat J: Arabidopsis ABA response gene ABI1: features of a calcium-modulated protein phosphatase. Science 264: 1448–1452 (1994).Google Scholar
  32. 32.
    Leung J, Merlot S, Giraudat J: The Arabidopsis abscisic acid-insensitive2 (ABI2) and ABI1 genes encode homologous protein phosphatases 2C involved in abscisic acid signal transduction. Plant Cell 9: 759–771 (1997).Google Scholar
  33. 33.
    Li J, Chory J: A putative leucine-rich repeat receptor kinase involved in brassinosteroid signal transduction. Cell 90: 929–938 (1997).Google Scholar
  34. 34.
    Luan S, Li W, Rusnak F, Assmann SM, Schreiber SL: Immunosuppressants implicate protein phosphatase regulation of K+ channels in guard cells. Proc Natl Acad Sci USA 90: 2202–2206 (1993).Google Scholar
  35. 35.
    Maeda T, Wurgler-Murphy SM, Saito H: A two-component system that regulates an osmosensing MAP kinase cascade in yeast. Nature 369: 242–245 (1994).Google Scholar
  36. 36.
    Mayer-Jaekel RE, Hemmings BA: Protein phosphatase 2A: a ‘ménage à trios’. Trends Cell Biol 4: 287–291 (1994).Google Scholar
  37. 37.
    McGowan CH, Cohen P: Protein phosphatase 2C from rabbit skeletal muscle and liver: an Mg2+ dependent enzyme. Meth Enzymol 159: 416–426 (1988).Google Scholar
  38. 38.
    McGrath JM, Jancso MM, Pichersky E: Duplicate sequences with a similarity to expressed genes in the genome of Arabidopsis thaliana. Theor Appl Genet 86: 880–888 (1993).Google Scholar
  39. 39.
    Merlot S, Giraudat J: Genetic analysis of abscisic acid signal transduction. Plant Physiol 114: 751–757 (1997).Google Scholar
  40. 40.
    Meskiene I, Bögre L, Glaser W, Balog J, Brandstötter M, Zwerger K, Ammerer G, Hirt H: MP2C, a plant protein phosphatase 2C, functions as a negative regulator of mitogenactivated protein kinase pathways in yeast and plants. Proc Natl Acad Sci USA 95: 1938–1943 (1998).Google Scholar
  41. 41.
    Meyer K, Leube MP, Grill E: A protein phosphatase 2C involved in ABA signal transduction in Arabidopsis thaliana. Science 264: 1452–1455 (1994).Google Scholar
  42. 42.
    Milarski KL, Saltiel AR: Expression of catalytically inactive Syp phosphatase in 3T3 cells blocks stimulation of mitogenactivated protein kinase by insulin. J Biol Chem 269: 21239–21243 (1994).Google Scholar
  43. 43.
    Moncrief ND, Kretsinger RH, Goodman M: Evolution of EFhand calcium-modulated proteins. I. Relationships based on amino acid sequences. J Mol Evol 30: 522–562 (1990).Google Scholar
  44. 44.
    Moore F, Weekes J, Hardie DG: Evidence that AMP triggers phosphorylation as well as direct allosteric activation of rat liver AMP-activated protein kinase. Eur J Biochem 199: 691–697 (1991).Google Scholar
  45. 45.
    Pei Z-M, Kuchitsu K, Ward JM, Schwarz M, Schroeder JI: Differential abscisic acid regulation of guard cell slow anion channels in Arabidopsis wild-type and abi1 and abi2 mutants. Plant Cell 9: 409–423 (1997).Google Scholar
  46. 46.
    Pickett FB, Meeks-Wagner DR: Seeing double: appreciating genetic redundancy. Plant Cell 7: 1347–1356 (1995).Google Scholar
  47. 47.
    Rodriguez PL, Benning G, Grill E: ABI2, a second protein phosphatase 2C involved in ABA signal transduction in Arabidopsis. FEBS Lett 421: 185–190 (1998).Google Scholar
  48. 48.
    Rodriguez PL, Leube M, Grill E: Molecular cloning in Arabidopsis thaliana of a new protein phosphatase 2C (PP2C) with homology to ABI1 and ABI2. Plant Mol Biol (1988), in press.Google Scholar
  49. 49.
    Schreiber SL: Immunophilin-sensitive phosphatase action in cell signaling pathways. Cell 70: 365–368 (1992).Google Scholar
  50. 50.
    Sheen J: Ca2+-dependent protein kinases and stress signal transduction in plants. Science 274: 1900–1902 (1996).Google Scholar
  51. 51.
    Sheen J: Mutational analysis of protein phosphatase 2C involved in abscisic acid signal transduction in higher plants. Proc Natl Acad Sci USA 95: 975–980 (1998).Google Scholar
  52. 52.
    Shenolikar S: Protein serine/threonine phosphatases: new avenues for cell regulation. Annu Rev Cell Biol 10: 55–86 (1994).Google Scholar
  53. 53.
    Shibasaki F, Price ER, Milan D, Mckeon F: Role of kinases and the phosphatase calcineurin in the nuclear shuttling of transcription factor NF-AT4. Nature 382: 370–373 (1996).Google Scholar
  54. 54.
    Shiozaki K, Russell P: Counteractive roles of protein phosphatase 2C (PP2C) and a MAP kinase kinase homolog in the osmoregulation of fission yeast. EMBO J 14: 492–502 (1995).Google Scholar
  55. 55.
    Smith RD, Walker JC: Plant protein phosphatases. Annu Rev Plant Physiol Plant Mol Biol 47: 101–125 (1996).Google Scholar
  56. 56.
    Song W-Y, Wang G-L-, Chen L-L, Kim H-S, Pi L-Y, Holsten T, Gardner J, Wang B, Zhao W-X, Zhu L-H, Fauquet C, Ronald P: A receptor kinase-like protein encoded by the rice disease resistance gene, Xa21. Science 270: 1804–1806 (1995).Google Scholar
  57. 57.
    Söderman E, Mattsson J, Engström P: The Arabidopsis homeobox gene ATHB-7 is induced by water deficit and by abscisic acid. Plant J 10: 375–381 (1996).Google Scholar
  58. 58.
    Stark MJR: Yeast protein serine/threonine phosphatases: multiple roles and diverse regulation. Yeast 12: 1647–1675 (1996).Google Scholar
  59. 59.
    Stone JM, Collinge MA, Smith RD, Horn MA, Walker JC: Interaction of a protein phosphatase with an Arabidopsis serinethreonine receptor kinase. Science 266: 793–795 (1994).Google Scholar
  60. 60.
    Strizhov N, Abraham E, Okresz L, Blickling S, Zilberstein A, Schell J, Koncz C, Szabados L: Differential expression of two P5CS genes controlling proline accumulation during saltstress requires ABA and is regulated by ABA1, ABI1 and AXR2 in Arabidopsis. Plant J 12: 557–569 (1997).Google Scholar
  61. 61.
    Sun H, Charles CH, Lau LF, Tonks NK: MKP-1 (3CH134), an immediate early gene product, is a dual specificity phosphatase that dephosphorylates MAP kinase in vivo. Cell 75: 487–493 (1993).Google Scholar
  62. 62.
    Tamura S, Lynch KR, Larner J, Fox J, Yasui A, Kikuchi K, Suzuki Y, Tsuiki S: Molecular cloning of rat type 2C (IA) protein phosphatase mRNA. Proc Natl Acad Sci USA 86: 1796–1800 (1989).Google Scholar
  63. 63.
    Torii KU, Mitsukawa N, Oosumi T, Matsuura Y, Yokoyama R, Whittier RF, Komeda Y: The Arabidopsis ERECTA gene encodes a putative receptor protein kinase with extracellular leucine-rich repeats. Plant Cell 8: 735–746 (1996).Google Scholar
  64. 64.
    Ullrich A, Sclessinger J: Signal transduction by receptors with tyrosine kinase activity. Cell 61: 203–212 (1990).Google Scholar
  65. 65.
    Vartanian N, Marcotte L, Giraudat J: Drought rhizogenesis in Arabidopsis thaliana. Plant Physiol 104: 761–767 (1994).Google Scholar
  66. 66.
    Walker JC: Receptor-like protein kinase genes of Arabidopsis thaliana. Plant J 3: 451–456 (1993).Google Scholar
  67. 67.
    Walker JC: Structure and function of the receptor-like protein kinases of higher plants. Plant Mol Biol 26: 1599–1609 (1994).Google Scholar
  68. 68.
    Williams RW, Wilson JM, Meyerowitz EM: A possible role for kinase-associated protein phosphatase in the Arabidopsis CLAVATA1 signaling pathway. Proc Natl Acad Sci USA 94: 10467–10472 (1997).Google Scholar

Copyright information

© Kluwer Academic Publishers 1998

Authors and Affiliations

  • Pedro L. Rodriguez
    • 1
  1. 1.Instituto de Biologia Molecular y Celular de PlantasUniversidad Politecnica – C.S.I.C., Camino de VeraValenciaSpain

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