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First published online September 16, 2002; 10.1105/tpc.002998

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The Plant Cell, Vol. 14, 2613-2626, October 2002, Copyright © 2002,
American Society of Plant Biologists

Signal-Mediated Depolymerization of Actin in Pollen during the Self-Incompatibility Response

Benjamin N. Snowmana, David R. Kovarb, Galina Shevchenkoa, Vernonica E. Franklin-Tong1,a and Christopher J. Staigerb

a School of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, United Kingdom
b Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907-1392

1 To whom correspondence should be addressed. E-mail v.e.franklin-tong{at}bham.ac.uk; fax 44-121-414-5925

Signal perception and the integration of signals into networks that effect cellular changes is essential for all cells. The self-incompatibility (SI) response in field poppy pollen triggers a Ca2+-dependent signaling cascade that results in the inhibition of incompatible pollen. SI also stimulates dramatic alterations in the actin cytoskeleton. By measuring the amount of filamentous (F-) actin in pollen before and during the SI response, we demonstrate that SI stimulates a rapid and large reduction in F-actin level that is sustained for at least 1 h. This represents quantitative evidence for stimulus-mediated depolymerization of F-actin in plant cells by a defined biological stimulus. Surprisingly, there are remarkably few examples of sustained reductions in F-actin levels stimulated by a biologically relevant ligand. Actin depolymerization also was achieved in pollen by treatments that increase cytosolic free Ca2+ artificially, providing evidence that actin is a target for the Ca2+ signals triggered by the SI response. By determining the cellular concentrations and binding constants for native profilin from poppy pollen, we show that profilin has Ca2+-dependent monomeric actin-sequestering activity. Although profilin is likely to contribute to stimulus-mediated actin depolymerization, our data suggest a role for additional actin binding proteins. We propose that Ca2+-mediated depolymerization of F-actin may be a mechanism whereby SI-induced tip growth inhibition is achieved.




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