A reassessment of the intervention of calmodulin in the regulation of stomatal movement

Physiologia Plantarum

Volumn 98, Issue 3, 1996, Pages 619-628

  Cotelle, Valérie ^a   Forestier, Cyrille ^a   Vavasseur, Alain ^a  

^a IRFM   (France)

Author keywords

Calcium; Calmodulin; Commelina communis; Guard cells; Protein phosphorylation; Stomata

Indexed keywords

EID: 0030484234     PISSN: 00319317     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1399-3054.1996.tb05719.x     Document Type: Article

References (46)

1. 2+-permeable slow vacuoïar ion channel of stomatal guard cells. - Plant Cell 7: 1473-1483.
2. 2+-pumping ATPase purified from Brassica oleracea L. - Plant Physiol. 100: 1670-1681.
3. Chanson, A. 1993. Active transport of proton and calcium in higher plant cells. - Plant Physiol. Biochem. 31: 943-955.
4. De Silva, D. L. R., Cox, R. C., Hetherington, A. M. & Mansfield, T. A. 1985. Suggested involvement of calcium and calmodulin in the response of stomata to abscisic acid. - New Phytol. 101: 555-564.
5. Donovan, N., Martin, S. & Donkin, M. E. 1985. Calmodulin binding drugs trifluoperazine and compound 48/80 modify stomatal responses of Commelina communis L. - J. Plant Physiol. 118: 177-187.
6. Fitzsimons, P. J. & Weyers, J. D. W. 1983. Separation and purification of protoplast types from Commelina communis L. leaf epidermis. - J. Exp. Bot. 34: 55-66.
7. Gietzen, K., Adamczyk-Engelmann, P., Wüthrich, A., Konstantinova, A. & Bader, H. 1983. Compound 48/80 is a selective and powerful inhibitor of calmodulin-regutated functions. - Biochim. Biophys. Acta 736: 109-118.
8. Gilroy, S., Hughes, W. A. & Trewavas, A. J. 1987. Calmodulin antagonists increase free cytosolic calcium levels in plant protoplasts in vivo. - FEBS Lett. 212: 133-137.
9. González-Darós, F., Carrasco-Luna, J., Calatayud, A., Salguero, J. & Valle-Tascon, S. 1993. Effects of calmodulin antagonists on auxin-stimulated proton extrusion in Avena sativa coleoptile segments. - Physiol. Plant. 87: 68-76.
10. Hagiwara, M., Inagaki, M. & Hidaka, H. 1987. Specific binding of novel compound, N-[2-(methylamino) ethyl]-5-isoquinolinesulfonamide (H-8) to the active site of cAMP-dependent protein kinase. - Mol. Pharmacol. 31: 523-528.
11. 2+-calmodulin-dependent protein kinase II by K252a and its derivative, KT5926. - Biochem. Biophys. Res. Commun. 181: 423-429.
12. Hedrich, R. & Neher, E. 1987. Cytoplasmic calcium regulates voltage-dependent ion channels in plant vacuoles. - Nature 329: 833-836.
13. 2+ and nucleotide dependent regulation of voltage dependent anion channels in the plasma membrane of guard cells. - EMBO J. 9: 3889-3892.
14. Hidaka, H. & Kobayashi, R. 1993. Use of protein (serine/threonine) kinase activators and inhibitors to study protein phosphorylation in intact cells. - In Protein Phosphorylation, A Practical Approach (D. G. Hardie, ed.), pp. 87-107. IRL Press at Oxford University Press, Oxford. ISBN 0-19-963306-1.
15. _ , Inagaki, M., Kawamoto, M. & Sasaki, Y. 1984. Isoquinoline sulfonamides, novel and potent inhibitors of cyclic nucleotide dependent protein kinase and protein kinase C. - Biochemistry 23: 5036-5041.
16. Hulen, D., Baron, A., Salisbury, J. & Clarke, M. 1991. Production and specificity of monoclonal antibodies against calmodulin from Dictyostelium discodeum. - Cell. Motil. Cytoskel. 18: 113-122.
17. Jablonsky, P. P., Grolig, F., Perkin, J. L. & Williamson, R. E. 1991. Properties of monoclonal antibodies to plant calmodulin. - Plant Sci. 76: 175-184.
18. Kase, H., Kazuyuki, I., Nakanishi, S., Matsuda, Y., Yamada, K., Takahashi, M., Murakata, C., Sato, A. & Kaneko, M. 1987. K-252 compounds, novel and potent inhibitors of protein kinase C and cyclic nucleotide-dependent protein kinases. - Biochem. Biophys. Res. Commun. 142: 436-440.
19. +-ATPase in guard cells of fava bean. - Plant Cell 7: 1333-1342.
20. Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. - Nature 227: 680-685.
21. Ling, V. & Assmann, S. M. 1992. Cellular distribution of calmodulin and calmodulin-binding proteins in Vicia faba L. - Plant Physiol. 100: 970-978.
22. +-ATPase from Vicia faba guard cells: Modulation by extracellular factors and seasonal changes. - Planta 188: 206-214.
23. 45Ca autoradiography on nitrocellulose membrane after sodium dodecyl sulfate gel electrophoresis. - J. Biochem. 95: 511-519.
24. Nakanishi, S., Yamada, K., Kase, H., Nakamura, S. & Nonomura, Y. 1988. K252a, a novel microbial product, inhibits smooth muscle myosin light chain kinase. - J. Biol. Chem. 263: 6215-6219.
25. _ , Yamada, K., Iwahashi, K., Kuroda, K. & Kase, H. 1990. KT5926, a potent and selective inhibitor of myosin light chain kinase. - Mol. Pharmacol. 37: 482-488.
26. Nejidat, A. 1987. Effect of ophiobolin A on stomatal movement: Role of calmodulin. - Plant Cell Physiol. 28: 455-460.
27. _ 1995. Possible involvement of calmodulin in the regulation of ATPase activity in guard cells. - Physiol. Plant. 94: 411-414.
28. Ohya, T. & Shimazaki, K. I. 1989. Profiles of proteins in guard-cells and mesophyll protoplasts from Vicia faba L. fractionated by sodium dodecylsulfate-polyacrylamide gel electrophoresis. - Plant Cell Physiol. 30: 783-787.
29. --sensitive anion channels in the Chara plasmalemma: A patch-clamp study. - Plant Cell Physiol. 34: 75-82.
30. Ranjeva, R. & Boudet, A. M. 1987. Phosphorylation of proteins in plants: Regulatory effects and potential involvement in stimulus/response coupling. - Annu. Rev. Plant Physiol. 38: 73-93.
31. Roberts, D. M. 1993. Protein kinases with calmodulin-like domains: Novel targets of calcium signals in plants. - Curr. Opin. Cell. Biol. 5: 242-246.
32. _ & Harmon, A. C. 1992. Calcium-modulated proteins: Targets of intracellular calcium signals in higher plants. - Annu. Rev. Plant Physiol. Plant Mol. Biol. 43: 375-414.
33. Roufogalis, B. D., Minocherhomjee, A. E. V. & Al-Jobore, A. 1983. Pharmacological antagonists of calmodulin. - Can. J. Biochem. Cell Biol. 61: 927-933.
34. Ruiz, L. P. & Mansfield, T. A. 1994. A postulated role for calcium oxalate in the regulation of calcium ions in the vicinity of stomatal guard cells. - New Phytol. 127: 473-481.
35. Saitoh, M., Ishikawa, T., Matsushima, S., Naka, M. & Hidaka, H. 1987. Selective inhibition of catalytic activity of smooth muscle myosin light chain kinase. - J. Biol. Chem. 262: 7796-7801.
36. Schmidt, C., Schelle, I., Liao, Y. J. & Schroeder, J. I. 1995. Strong regulation of slow anion channels and abscisic acid signaling in guard cells by phosphorylation and dephosphorylation events. - Proc. Natl. Acad. Sci. USA 92: 9535-9539.
37. 2+/calmodulin-dependent protein kinases. - Curr. Opin. Cell Biol. 5: 247-253.
38. Schulz-Lessdorf, B. & Hedrich, R. 1995. Protons and calcium modulate SV-type channels in the vacuolar-lysosomal compartement - channel interaction with calmodulin inhibitors. - Planta 197: 655-671.
39. 2+ and EGTA on stomatal movements in Commelina communis L. - Plant Physiol. 79: 1003-1005.
40. Shimazaki, K. I., Kinoshita, T. & Nishimura, M. 1992. Involvement of calmodulin and calmodulin-dependent myosin light chain kinase in blue light-dependent proton pumping by guard cell protoplasts from Vicia faba L. - Plant Physiol. 99: 1416-1421.
41. _ , Omasa, K., Kinoshita, T. & Nishimura, M. 1993. Properties of the signal transduction pathway in the blue light response of stomatal guard cells of Vicia faba and Commelina benghalensis. - Plant Cell Physiol. 34: 1321-1327.
42. Takezawa, D., Liu, Z. H., An, G. & Poovaiah, B. W. 1995. Calmodulin gene family in potato: Developmental and touch-induced expression of the mRNA encoding a novel isoform. - Plant Mol. Biol. 27: 693-703.
43. 2+/calmodulin-dependent protein kinase II. - J. Biol. Chem. 265:4315-4320.
44. Vavasseur, A., Lascève, G. & Cousson, A. 1995. Guard cell responses to potassium ferricyanide. - Physiol. Plant. 93: 253-258.
45. + channels and calcium-induced calcium release by slow vacuolar ion channels in guard cell vacuoles implicated in the control of stomatal closure. - Plant Cell 6: 669-683.
46. Weyers, J. & Meidner, H. 1990. Epidermal strips. - In Methods in Stomatal Research, pp. 135-137. Longman Scientific & Technical, London. ISBN 0-582-03483-3.