Regulation of the Pollen-Specific Actin-Depolymerizing Factor LlADF1
| Autor: | Richard G. Anthony, John H. Doonan, Alan G. Weeds, Patrick J. Hussey, Andrei Smertenko, Ellen G. Allwood, Bjørn K. Drøbak, Stefanie Reichelt |
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| Rok vydání: | 2002 |
| Předmět: |
Arabidopsis
Arp2/3 complex Saccharomyces cerevisiae macromolecular substances Plant Science medicine.disease_cause Zea mays Magnoliopsida Gene Expression Regulation Plant Two-Hybrid System Techniques Pollen otorhinolaryngologic diseases medicine Cloning Molecular Phosphorylation Conserved Sequence Cytoskeleton Phospholipids Phylogeny Actin Plant Proteins biology Arabidopsis Proteins Brassica napus Microfilament Proteins food and beverages Actin remodeling Cell Biology Hydrogen-Ion Concentration Actin cytoskeleton Actins Cell biology Destrin Actin Depolymerizing Factors Profilin Actin depolymerizing factor biology.protein Pollen tube Lilium Carrier Proteins Research Article |
| Zdroj: | The Plant Cell. 14:2915-2927 |
| ISSN: | 1532-298X 1040-4651 |
| DOI: | 10.1105/tpc.005363 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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