ArticlePLoS biology2023
Activation of actin-depolymerizing factor by CDPK16-mediated phosphorylation promotes actin turnover in Arabidopsis pollen tubes.
Article in PLoS biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 15 citations in OpenAlex.
- Phosphorylation at the stigmatic gate: how FERONIA regulates actin organization to control pollen hydration.Plant physiology · 2026Article
- Cytoskeletal control of development and environmental adaptation in plants.Science China. Life sciences · 2026Review
- Heat-stable protein PGSL1 enhances pollen germination and tube growth at high temperature.Nature communications · 2025Article
- Functional Characterization ofInternational journal of molecular sciences · 2025Article
- Autophagy modulates Arabidopsis male gametophyte fertility and controls actin organization.Nature communications · 2024Article
- Evolution of the thermostability of actin-depolymerizing factors enhances the adaptation of pollen germination to high temperature.The Plant cell · 2024Article
- Actin-depolymerizing factors 8 and 11 promote root hair elongation at high pH.Plant communications · 2024Article
- Differential sensitivity of ADF isovariants to a pH gradient promotes pollen tube growth.The Journal of cell biology · 2023Article
- Actin-Depolymerizing Factor Subgroup I Members Negatively Regulate Pollen Tube Growth in Fortunella hindsii.Physiologia plantarumArticle
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
As the stimulus-responsive mediator of actin dynamics, actin-depolymerizing factor (ADF)/cofilin is subject to tight regulation. It is well known that kinase-mediated phosphorylation inactivates ADF/cofilin. Here, however, we found that the activity of Arabidopsis ADF7 is enhanced by CDPK16-mediated phosphorylation. We found that CDPK16 interacts with ADF7 both in vitro and in vivo, and it enhances ADF7-mediated actin depolymerization and severing in vitro in a calcium-dependent manner. Accordingly, the rate of actin turnover is reduced in cdpk16 pollen and the amount of actin filaments increases significantly at the tip of cdpk16 pollen tubes. CDPK16 phosphorylates ADF7 at Serine128 both in vitro and in vivo, and the phospho-mimetic mutant ADF7S128D has enhanced actin-depolymerizing activity compared to ADF7. Strikingly, we found that failure in the phosphorylation of ADF7 at Ser128 impairs its function in promoting actin turnover in vivo, which suggests that this phospho-regulation mechanism is biologically significant. Thus, we reveal that CDPK16-mediated phosphorylation up-regulates ADF7 to promote actin turnover in pollen.
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