| Literature DB >> 12417710 |
Ellen G Allwood1, Richard G Anthony, Andrei P Smertenko, Stefanie Reichelt, Bjorn K Drobak, John H Doonan, Alan G Weeds, Patrick J Hussey.
Abstract
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 approximately 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.Entities:
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Year: 2002 PMID: 12417710 PMCID: PMC152736 DOI: 10.1105/tpc.005363
Source DB: PubMed Journal: Plant Cell ISSN: 1040-4651 Impact factor: 11.277