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Plant and Cell Physiology, 2001, Vol. 42, No. 9 912-922
© 2001 Oxford University Press

Mastoparan Alters Subcellular Distribution of Profilin and Remodels F-Actin Cytoskeleton in Cells of Maize Root Apices

Frantisek Baluska1,2,4, Matthias von Witsch1,5, Mechthild Peters1, Andrej Hlavacka3 and Dieter Volkmann1

1 Botanisches Institut, Rheinische Friedrich-Wilhelms-Universität Bonn, Department of Plant Cell Biology, Kirschallee 1, D-53115 Bonn, Germany 2Institute of Botany, Slovak Academy of Sciences, Dúbravská cesta 14, SK-84223 Bratislava, Slovakia 3 Department of Plant Physiology, Comenius University, Mlynská dolina, SK-84512, Bratislava, Slovakia

Indirect immunofluorescence localization of profilin in cells of maize root apices revealed that this abundant protein was present both in the cytoplasm and within nuclei. Nucleo-cytoplasmic partitioning of profilin exhibits tissue-specific and developmental features. Mastoparan-mediated activation of heterotrimeric G-proteins, presumably through triggering a phosphoinositide-signaling pathway based on phosphatidylinositol-4,5-bisphosphate (PIP2), induced relocalization of profilin from nuclei into the cytoplasm of root apex cells. In contrast, PIP2 accumulated within nuclei of mastoparan-treated root cells. Intriguingly, cytoplasmic accumulation of profilin was associated with remodeling of F-actin arrays in root apex cells. Specifically, dense F-actin networks were dismantled and distinct actin patches became associated with the periphery of small vacuoles. On the other hand, disruption of F-actin with the G-actin sequestering agent latrunculin B does not affect the subcellular distribution of profilin or PIP2. These data suggest that nuclear profilin can mediate a stimulus–response action on the actin cytoskeleton which is somehow linked to a phosphoinositide-signaling cascade.

4 Corresponding author: Email, baluska@uni-bonn.de; Fax, +49-228-739004.

5 Present address: Purdue University, Department of Biological Sciences, West Lafayette, IN 47907-1392, U.S.A.


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