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Regulation of the pollen-specific actin-depolymerizing factor LlADF1.

Ellen G Allwood¹, Richard G Anthony, Andrei P Smertenko

¹Integrative Cell Biology Laboratory, School of Biological and Biomedical Sciences, University of Durham, South Road, Durham DH1 3LE, United Kingdom.

|November 6, 2002

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Lily pollen actin-depolymerizing factor (ADF) LlADF1 and actin-interacting protein (AIP1) work together to remodel actin filaments. This interaction is crucial for pollen grains entering and exiting dormancy, impacting plant reproduction.

Area of Science:

Plant biology
Cell biology
Molecular biology

Background:

Pollen tube growth relies on a dynamic actin cytoskeleton.
Actin-regulating proteins are essential for this process.

Purpose of the Study:

To investigate the regulation of lily pollen-specific actin-depolymerizing factor (ADF), LlADF1.
To understand the role of actin-interacting protein (AIP1) in conjunction with LlADF1.

Main Methods:

Biochemical assays to determine LlADF1 activity.
Identification of plant homologs of actin-interacting protein (AIP1).
Localization studies of LlADF1 and pollen AIP1 in pollen grains and tubes.

Main Results:

LlADF1's actin binding and depolymerization activity is pH-sensitive and inhibited by phosphoinositides, but not phosphorylation.

Related Experiment Videos

A plant AIP1 homolog significantly enhances LlADF1's F-actin depolymerization activity.

Both LlADF1 and pollen AIP1 bind F-actin in pollen grains but are primarily cytoplasmic in pollen tubes.

Conclusions:

LlADF1 and pollen AIP1 cooperate to remodel actin filaments.
This remodeling is proposed to occur as pollen grains enter and exit dormancy.