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Plant Cell Advance Online Publication
Published on October 15, 2002; 10.1105/tpc.005363

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Received June 18, 2002
Accepted August 22, 2002

Regulation of the Pollen-Specific Actin-Depolymerizing Factor LlADF1

Ellen G. Allwood 1, Richard G. Anthony 2, Andrei P. Smertenko 1, Stefanie Reichelt 3, Bjorn K. Drobak 4, John H. Doonan 4, Alan G. Weeds 3, and Patrick J. Hussey 1*

1 Integrative Cell Biology Laboratory, School of Biological and Biomedical Sciences, University of Durham, South Road, Durham DH1 3LE, United Kingdom
2 School of Biological Sciences, Royal Holloway, University of London, Egham Hill, Egham, Surrey TW20 0EX, United Kingdom
3 Medical Research Council Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, United Kingdom
4 Department of Cell Biology, John Innes Centre, Colney Lane, Norwich NR4 7UH, United Kingdom

* To whom correspondence should be addressed. E-mail: p.j.hussey{at}durham.ac.uk.

Pollen tube growth is dependent on a dynamic actin cytoskeleton, suggesting that actin-regulating proteins are involved. We have examined the regulation of the lily pollen-specific actin-depolymerizing factor (ADF) LlADF1. Its actin binding and depolymerizing activity is pH sensitive, inhibited by certain phosphoinositides, but not controlled by phosphorylation. Compared with its F-actin binding properties, its low activity in depolymerization assays has been used to explain why pollen ADF decorates F-actin in pollen grains. This low activity is incompatible with a role in increasing actin dynamics necessary to promote pollen tube growth. We have identified a plant homolog of actin-interacting protein, AIP1, which enhances the depolymerization of F-actin in the presence of LlADF1 by ~60%. Both pollen ADF and pollen AIP1 bind F-actin in pollen grains but are mainly cytoplasmic in pollen tubes. Our results suggest that together these proteins remodel actin filaments as pollen grains enter and exit dormancy.




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