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. 1996 Mar;110(3):965–970. doi: 10.1104/pp.110.3.965

Auxins and Cytokinins as Antipodal Modulators of Elasticity within the Actin Network of Plant Cells.

S Grabski 1, M Schindler 1
PMCID: PMC157796  PMID: 12226233

Abstract

The cytoskeleton of plant and animal cells serves as a transmitter, transducer, and effector of cell signaling mechanisms. In plants, pathways for proliferation, differentiation, intracellular vesicular transport, cell-wall biosynthesis, symbiosis, secretion, and membrane recycling depend on the organization and dynamic properties of actin- and tubulin-based structures that are either associated with the plasma membrane or traverse the cytoplasm. Recently, a new in vivo cytoskeletal assay (cell optical displacement assay) was introduced to measure the tension within subdomains (cortical, transvacuolar, and perinuclear) of the actin network in living plant cells. Cell optical displacement assay measurements within soybean (Glycine max [L.]) root cells previously demonstrated that lipophilic signals, e.g. linoleic acid and arachidonic acid or changes in cytoplasmic pH gradients, could induce significant reductions in the tension within the actin network of transvacuolar strands. In contrast, enhancement of cytoplasmic free Ca2+ resulted in an increase in tension. In the present communication we have used these measurements to show that a similar antipodal pattern of activity exists for auxins and cytokinins (in their ability to modify the tension within the actin network of plant cells). It is suggested that these growth substances exert their effect on the cytoskeleton through the activation of signaling cascades, which result in the production of lipophilic and ionic second messengers, both of which have been demonstrated to directly effect the tension within the actin network of soybean root cells.

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Selected References

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  1. Adams D. S. Mechanisms of cell shape change: the cytomechanics of cellular response to chemical environment and mechanical loading. J Cell Biol. 1992 Apr;117(1):83–93. doi: 10.1083/jcb.117.1.83. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Adams R. J., Pollard T. D. Binding of myosin I to membrane lipids. Nature. 1989 Aug 17;340(6234):565–568. doi: 10.1038/340565a0. [DOI] [PubMed] [Google Scholar]
  3. Ashkin A., Dziedzic J. M. Internal cell manipulation using infrared laser traps. Proc Natl Acad Sci U S A. 1989 Oct;86(20):7914–7918. doi: 10.1073/pnas.86.20.7914. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. David-Pfeuty T., Singer S. J. Altered distributions of the cytoskeletal proteins vinculin and alpha-actinin in cultured fibroblasts transformed by Rous sarcoma virus. Proc Natl Acad Sci U S A. 1980 Nov;77(11):6687–6691. doi: 10.1073/pnas.77.11.6687. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Edelman G. M. Surface modulation in cell recognition and cell growth. Science. 1976 Apr 16;192(4236):218–226. doi: 10.1126/science.769162. [DOI] [PubMed] [Google Scholar]
  6. Ettlinger C., Lehle L. Auxin induces rapid changes in phosphatidylinositol metabolites. Nature. 1988 Jan 14;331(6152):176–178. doi: 10.1038/331176a0. [DOI] [PubMed] [Google Scholar]
  7. Gibbon B. C., Kropf D. L. Cytosolic pH Gradients Associated with Tip Growth. Science. 1994 Mar 11;263(5152):1419–1421. doi: 10.1126/science.263.5152.1419. [DOI] [PubMed] [Google Scholar]
  8. Goldschmidt-Clermont P. J., Machesky L. M., Baldassare J. J., Pollard T. D. The actin-binding protein profilin binds to PIP2 and inhibits its hydrolysis by phospholipase C. Science. 1990 Mar 30;247(4950):1575–1578. doi: 10.1126/science.2157283. [DOI] [PubMed] [Google Scholar]
  9. Grabski S., Schindler M. Aluminum Induces Rigor within the Actin Network of Soybean Cells. Plant Physiol. 1995 Jul;108(3):897–901. doi: 10.1104/pp.108.3.897. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Hahm S. H., Saunders M. J. Cytokinin increases intracellular Ca2+ in Funaria: detection with Indo-1. Cell Calcium. 1991 Nov;12(10):675–681. doi: 10.1016/0143-4160(91)90037-f. [DOI] [PubMed] [Google Scholar]
  11. Herman B., Pledger W. J. Platelet-derived growth factor-induced alterations in vinculin and actin distribution in BALB/c-3T3 cells. J Cell Biol. 1985 Apr;100(4):1031–1040. doi: 10.1083/jcb.100.4.1031. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Janmey P. A., Euteneuer U., Traub P., Schliwa M. Viscoelastic properties of vimentin compared with other filamentous biopolymer networks. J Cell Biol. 1991 Apr;113(1):155–160. doi: 10.1083/jcb.113.1.155. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Kropf D. L., Berge S. K., Quatrano R. S. Actin Localization during Fucus Embryogenesis. Plant Cell. 1989 Feb;1(2):191–200. doi: 10.1105/tpc.1.2.191. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Landreth G. E., Williams L. K., Rieser G. D. Association of the epidermal growth factor receptor kinase with the detergent-insoluble cytoskeleton of A431 cells. J Cell Biol. 1985 Oct;101(4):1341–1350. doi: 10.1083/jcb.101.4.1341. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Luna E. J., Hitt A. L. Cytoskeleton--plasma membrane interactions. Science. 1992 Nov 6;258(5084):955–964. doi: 10.1126/science.1439807. [DOI] [PubMed] [Google Scholar]
  16. Metcalf T. N., 3rd, Villanueva M. A., Schindler M., Wang J. L. Monoclonal antibodies directed against protoplasts of soybean cells: analysis of the lateral mobility of plasma membrane-bound antibody MVS-1. J Cell Biol. 1986 Apr;102(4):1350–1357. doi: 10.1083/jcb.102.4.1350. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Metcalf T. N., 3rd, Wang J. L., Schubert K. R., Schindler M. Lectin receptors on the plasma membrane of soybean cells. Binding and lateral diffusion of lectins. Biochemistry. 1983 Aug 2;22(16):3969–3975. doi: 10.1021/bi00285a037. [DOI] [PubMed] [Google Scholar]
  18. Morré D. J., Gripshover B., Monroe A., Morré J. T. Phosphatidylinositol turnover in isolated soybean membranes stimulated by the synthetic growth hormone 2,4-dichlorophenoxyacetic acid. J Biol Chem. 1984 Dec 25;259(24):15364–15368. [PubMed] [Google Scholar]
  19. Picton J. M., Steer M. W. Membrane recycling and the control of secretory activity in pollen tubes. J Cell Sci. 1983 Sep;63:303–310. doi: 10.1242/jcs.63.1.303. [DOI] [PubMed] [Google Scholar]
  20. Rayle D. L., Cleland R. E. The Acid Growth Theory of auxin-induced cell elongation is alive and well. Plant Physiol. 1992 Aug;99(4):1271–1274. doi: 10.1104/pp.99.4.1271. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Ridley A. J., Hall A. The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell. 1992 Aug 7;70(3):389–399. doi: 10.1016/0092-8674(92)90163-7. [DOI] [PubMed] [Google Scholar]
  22. Saunders M. J., Hepler P. K. Calcium antagonists and calmodulin inhibitors block cytokinin-induced bud formation in Funaria. Dev Biol. 1983 Sep;99(1):41–49. doi: 10.1016/0012-1606(83)90252-x. [DOI] [PubMed] [Google Scholar]
  23. Saunders M. J., Hepler P. K. Calcium ionophore a23187 stimulates cytokinin-like mitosis in funaria. Science. 1982 Sep 3;217(4563):943–945. doi: 10.1126/science.217.4563.943. [DOI] [PubMed] [Google Scholar]
  24. Scherer G. F., André B. A rapid response to a plant hormone: auxin stimulates phospholipase A2 in vivo and in vitro. Biochem Biophys Res Commun. 1989 Aug 30;163(1):111–117. doi: 10.1016/0006-291x(89)92106-2. [DOI] [PubMed] [Google Scholar]
  25. Schliwa M., Nakamura T., Porter K. R., Euteneuer U. A tumor promoter induces rapid and coordinated reorganization of actin and vinculin in cultured cells. J Cell Biol. 1984 Sep;99(3):1045–1059. doi: 10.1083/jcb.99.3.1045. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Schumaker K. S., Gizinski M. J. Cytokinin stimulates dihydropyridine-sensitive calcium uptake in moss protoplasts. Proc Natl Acad Sci U S A. 1993 Dec 1;90(23):10937–10941. doi: 10.1073/pnas.90.23.10937. [DOI] [PMC free article] [PubMed] [Google Scholar]

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