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. 1995 Oct;109(2):491–497. doi: 10.1104/pp.109.2.491

Induction of Stomatal Closure by Vanadate or a Light/Dark Transition Involves Ca2+-Calmodulin-Dependent Protein Phosphorylations.

A Cousson 1, V Cotelle 1, A Vavasseur 1
PMCID: PMC157611  PMID: 12228607

Abstract

Previous studies indicate that a continual source of adenosine 5[prime]-triphosphate is required for both opening and closing of stomata. However, vanadate (Na3VO4 at 500 [mu]M) as well as a light/dark transition induced stomatal closing in epidermal peels of Commelina communis L., showing that the stoppage or even the decrease of the activity of the plasma membrane H+-adenosine 5[prime]-triphosphatase is sufficient to induce stomatal closure. Furthermore, stomatal closing in response to Na3VO4 or a light/dark transition was suppressed by inhibitors of metabolism (10 [mu]M carbonyl cyanide m-chlorophenylhydrazone) and of protein kinases (20 [mu]M 1-[5-iodonaphthalene-1-sulfonyl]-1H-hexa-hydro-1,4-diaz-epine), calmodulin antagonists (20 [mu]M N-[6-aminohexyl]-5-chloro-1-naphthalenesulfonamide), and the anion channel blocker 5-nitro-2,3-phenylpropyllamino benzoic acid (50 [mu]M). These data suggest that the slow, outward rectifying anion channel, whose opening would be related to the membrane potential, and at least one step requiring a protein phosphorylation by a Ca2+-calmodulin-dependent protein kinase of the myosin light chain kinase type might be implicated in the induction of stomatal closing by vanadate or a light/dark transition.

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Selected References

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  1. Assmann S. M. Signal transduction in guard cells. Annu Rev Cell Biol. 1993;9:345–375. doi: 10.1146/annurev.cb.09.110193.002021. [DOI] [PubMed] [Google Scholar]
  2. Gallagher S. R., Leonard R. T. Effect of vanadate, molybdate, and azide on membrane-associated ATPase and soluble phosphatase activities of corn roots. Plant Physiol. 1982 Nov;70(5):1335–1340. doi: 10.1104/pp.70.5.1335. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. HEYTLER P. G. uncoupling of oxidative phosphorylation by carbonyl cyanide phenylhydrazones. I. Some characteristics of m-Cl-CCP action on mitochondria and chloroplasts. Biochemistry. 1963 Mar-Apr;2:357–361. doi: 10.1021/bi00902a031. [DOI] [PubMed] [Google Scholar]
  4. Hedrich R., Busch H., Raschke K. Ca2+ and nucleotide dependent regulation of voltage dependent anion channels in the plasma membrane of guard cells. EMBO J. 1990 Dec;9(12):3889–3892. doi: 10.1002/j.1460-2075.1990.tb07608.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Hidaka H., Yamaki T., Naka M., Tanaka T., Hayashi H., Kobayashi R. Calcium-regulated modulator protein interacting agents inhibit smooth muscle calcium-stimulated protein kinase and ATPase. Mol Pharmacol. 1980 Jan;17(1):66–72. [PubMed] [Google Scholar]
  6. Lemtiri-Chlieh F., MacRobbie E. A. Role of calcium in the modulation of Vicia guard cell potassium channels by abscisic acid: a patch-clamp study. J Membr Biol. 1994 Jan;137(2):99–107. doi: 10.1007/BF00233479. [DOI] [PubMed] [Google Scholar]
  7. Serrano E. E., Zeiger E., Hagiwara S. Red light stimulates an electrogenic proton pump in Vicia guard cell protoplasts. Proc Natl Acad Sci U S A. 1988 Jan;85(2):436–440. doi: 10.1073/pnas.85.2.436. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Shimazaki K., Kinoshita T., Nishimura M. Involvement of Calmodulin and Calmodulin-Dependent Myosin Light Chain Kinase in Blue Light-Dependent H Pumping by Guard Cell Protoplasts from Vicia faba L. Plant Physiol. 1992 Aug;99(4):1416–1421. doi: 10.1104/pp.99.4.1416. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Somlyo A. P., Somlyo A. V. Signal transduction and regulation in smooth muscle. Nature. 1994 Nov 17;372(6503):231–236. doi: 10.1038/372231a0. [DOI] [PubMed] [Google Scholar]

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