Skip to main content
Log in

Abscisic acid-induced gene-expression requires the activity of protein(s) sensitive to the protein-tyrosine phosphatase inhibitor phenylarsine oxide

  • Published:
Plant Growth Regulation Aims and scope Submit manuscript

Abstract

Abscisic acid-induced gene-expression requires the activity of protein(s) sensitive to the protein-tyrosine phosphatase inhibitor phenylarsine oxide. It is generally accepted that phosphorylation/dephosphorylation of proteins plays an important role in signal transduction cascades. evidence is now accumulating that for plants the same holds true. To study the role of phosphorylation in ABA signal transduction, we used six different compounds which were reported to inhibit phosphatase action. Three of these inhibitors: phenylarsine oxide (PAO), Calyculin A (CA) and Okadaic Acid (OA) appeared capable of inhibiting ABA-induced gene-expression. The same three inhibitors are shown to bring about hyperphosphorylation of two approximately 40 kDa proteins, present in the membrane-bound fraction of barley aleurone cells. The other three inhibitors had no visible effect on the phosphorylation status of the barley proteins. The hyperphosphorylation of the two 40 kDa proteins coincided with an increase of tyrosine-phosphorylation of two 40 kDa proteins with different pI, as determined with anti-phosphotyrosine antibodies.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

References

  1. Anderberg, RJ and Walker-Simmons, MK (1992) Isolation of a wheat cDNA clone for an abscisic acid-inducible transcript with homology to protein kinases. Proc Natl Acad Sci USA 89: 10183–10187

    PubMed  Google Scholar 

  2. Biolan, C and Takai, A (1988) Inhibitory effect of a marinesponge toxin, okadaic acid, on protein phosphatases. Biochem J 256: 283–290

    PubMed  Google Scholar 

  3. Damuni, Z (1990) Inactivation of bovine kidney cytosolic protamine kinase by catalytic subunit of protein phosphatase—ZA. Biochem Biophys Res Commun 166: 449–456

    PubMed  Google Scholar 

  4. Das, OP and Henderson, E (1983) A novel technique for gentle lysis of eukaryotic cells. Isolation of plasma membrane from Dictostelium discodeum. Biochem Biophys Acta 736: 45–56

    Google Scholar 

  5. Dayani, N, McNaught, RW, Shenolikar, S and Smith, RG (1990) Receptor interconversion model of hormone action 2. Requirement of both kinase and phosphatase activation for conferring estrogen binding activity to the estrogen receptor. Biochemistry 29: 2691–2698

    PubMed  Google Scholar 

  6. Felix, G, Regenass, M, Spanu, P and Boller, T (1994) The protein phosphatase inhibitor Calyculin A mimics elicitor action in plant cells and rapidly induces hyperphosphorylation of specific proteins as revealed by pulse labelling with [33P]phosphate. proc Natl Acad Sci USA 91: 952–956

    PubMed  Google Scholar 

  7. Garcia-Moralez, P, Minami, Y, Luong, EL, Klausner, RD and Samelson, LE (1990) Tyrosine phosphorylation in T-cells is regulated by phosphatase activity: studies with phenylarsine oxide. Proc Natl Acad Sci USA 87: 9255–9259

    PubMed  Google Scholar 

  8. Grosskopf, DG, Felix, G and Boller, T (1990) K252a inhibits the response of tomato cells to fungal elicitors in vivo and their microsomal protein kinase. FEBS Lett 275: 177–180

    Article  PubMed  Google Scholar 

  9. Gruol, DJ and Wolfe, KA (1990) Transformation of glucocorticoid receptors bound to the antagonist RU 486: effects of alkaline phosphatase. Biochemistry 29: 7958–7966

    PubMed  Google Scholar 

  10. Haystead, TAJ, Sim, ATR, Carling, D, Honnor, RC, Tsukitani, Y, Cohen, P and Hardie, DG (1989) Effects of the tumour promoter okadaic acid on intracellular protein phosphorylation and metabolism. Nature 337: 78–81

    Article  PubMed  Google Scholar 

  11. Heimovaara-Dijkstra, S, Van Duijn, B, Libbenga, KR, Heidekamp, F and Wang, M (1994) Abscisic acid-induced membrane potential changes in barley aleurone protoplasts: a possible relevance for the regulation of rab gene expression. Plant Cell Physiol 35: 743–750

    Google Scholar 

  12. Jonak, C, Herberle-Bors, E and Hirt, H (1994) Map kinases: Universal multi-purpose signalling tools. Plant Mol Biol 24: 407–416

    PubMed  Google Scholar 

  13. Klein, P, Vaughan, B, Berleis, J and Devreotes, PN (1987) The surface cyclic AMP receptor in Dictyostelium. J Biol Chem 262: 358–364

    PubMed  Google Scholar 

  14. Koontz, DA and Choi, JH (1993) Protein phosphorylation in carrot somatic embryos in response to abscisic acid. Plant Physiol Biochem 31: 95–102

    Google Scholar 

  15. Leammli, UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680–685

    PubMed  Google Scholar 

  16. Leung, J, Bouvier-Durand, M, Morris, PC, Guerrier, D, Chefdor, F and Giraudat, J (1994) Arabidopsis ABA response gene ABII: features of a calcium-modulated protein phosphatase. Science 264: 1448–1452

    PubMed  Google Scholar 

  17. Medema, RH, Burgering, BMT and Bos, JL (1991) Insulin-induced p21 ras activation does not require protein kinase C, but a protein sensitive to phenylarsine oxide. J Biol Chem 266: 21186–21189

    PubMed  Google Scholar 

  18. Meyer, K, Leube, MP and Grill, E (1994) A protein phosphatase 2C involved in ABA signal transduction in Arabidopsis thaliana. Science 264: 1452–1455

    PubMed  Google Scholar 

  19. Olah, Z and Kiss, Z (1986) Occurrence of lipid and phorbolester activated protein kinase in wheat cells. FEBS Lett 195: 33–37

    Article  Google Scholar 

  20. Raz, V and Fluhr, R (1993) Ethylene signal is transduced via protein phosphorylation events in plants. Plant Cell 5: 523–530

    Article  PubMed  Google Scholar 

  21. Rundle, SJ, Nashrallah, ME and Nashrallah, JB (1993) Effects of inhibitors of protein serine/threonine phosphatases on pollination in Brassica. Plant Physiol 103: 1165–1171

    PubMed  Google Scholar 

  22. Veluthambi, K and Poovaiah, BW (1986) In vitro and in vivo protein phosphorylation in Avena sativa. L. coleoptiles. Plant Physiol 81: 836–841

    PubMed  Google Scholar 

  23. Vera-Estalla, R, Barkla, BJ, Higgins, VJ and Blumwald, E (1994) Plant defence response to fungal pathogens. Plant Physiol 104: 209–215

    PubMed  Google Scholar 

  24. Verhey, SD and Lomax, TL (1993) Signal transduction in vascular plants. Plant Growth Regul 12: 179–195

    Article  Google Scholar 

  25. Wang, M, Van Duijn, B and Schram, A (1991) Abscisic acid induces a cytosolic calcium decrease in barley aleurone protoplasts. FEBS lett 278: 69–74

    Article  PubMed  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Heimovaara-Dijkstra, S., Nieland, T.J.F., van der Meulen, R.M. et al. Abscisic acid-induced gene-expression requires the activity of protein(s) sensitive to the protein-tyrosine phosphatase inhibitor phenylarsine oxide. Plant Growth Regul 18, 115–123 (1996). https://doi.org/10.1007/BF00028496

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00028496

Key words

Navigation