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Regulation of the pollen-specific actin-depolymerizing factor LIADF1

Allwood, E.G.; Anthony, R.G.; Smertenko, A.P.; Reichelt, S.; Drobak, B.K.; Doonan, J.H.; Weeds, A.G.; Hussey, P.J.


E.G. Allwood

R.G. Anthony

A.P. Smertenko

S. Reichelt

B.K. Drobak

J.H. Doonan

A.G. Weeds


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.

Journal Article Type Article
Publication Date Nov 1, 2002
Deposit Date May 17, 2007
Journal Plant Cell
Print ISSN 1040-4651
Electronic ISSN 1532-298X
Publisher Oxford University Press
Peer Reviewed Peer Reviewed
Volume 14
Issue 11
Pages 2915-2927
Public URL