ArticleThe Plant cell2010
Arabidopsis VILLIN5, an actin filament bundling and severing protein, is necessary for normal pollen tube growth.
Article in The Plant cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.
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Who cites it
80 citing papers in PubMed, 148 citations in OpenAlex.
- Unconventional vesicle transport driven by formin-actin-myosin working system during pollen germination.Science advances · 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
- Dynamics of Actin Filaments Play an Important Role in Root Hair Growth under Low Potassium Stress inInternational journal of molecular sciences · 2024Article
- Genome-Wide Analysis ofCurrent issues in molecular biology · 2024Article
- Exploring the Role of the Plant Actin Cytoskeleton: From Signaling to Cellular Functions.International journal of molecular sciences · 2023Review
- Genome-Wide Identification and Expression Analysis of thePlants (Basel, Switzerland) · 2023Article
- VILLIN2 regulates cotton defense against Verticillium dahliae by modulating actin cytoskeleton remodeling.Plant physiology · 2023Article
- Identification of Candidate Genes Involved in the Determinism of Pollen Grain Aperture Morphology by Comparative Transcriptome Analysis in Papaveraceae.Plants (Basel, Switzerland) · 2023Article
- Activation of actin-depolymerizing factor by CDPK16-mediated phosphorylation promotes actin turnover in Arabidopsis pollen tubes.PLoS biology · 2023Article
- The Cytoskeleton in Plant Immunity: Dynamics, Regulation, and Function.International journal of molecular sciences · 2022Review
- Let's shape again: the concerted molecular action that builds the pollen tube.Plant reproduction · 2022Review
- MPK3- and MPK6-mediated VLN3 phosphorylation regulates actin dynamics during stomatal immunity in Arabidopsis.Nature communications · 2021Article
- Quantitative cell biology of tip growth in moss.Plant molecular biology · 2021Review
- MicroRNA Omics Analysis ofBiomolecules · 2021Article
- The quest for the central players governing pollen tube growth and guidance.Plant physiology · 2021Review
- Pluronic F-68 Improves Callus Proliferation of Recalcitrant Rice CultivarFrontiers in plant science · 2021Article
- Bundling up the Role of the Actin Cytoskeleton in Primary Root Growth.Frontiers in plant science · 2021Review
- Decoding Heavy Metal Stress Signalling in Plants: Towards Improved Food Security and Safety.Plants (Basel, Switzerland) · 2020Review
20 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
11 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A dynamic actin cytoskeleton is essential for pollen germination and tube growth. However, the molecular mechanisms underlying the organization and turnover of the actin cytoskeleton in pollen remain poorly understood. Villin plays a key role in the formation of higher-order structures from actin filaments and in the regulation of actin dynamics in eukaryotic cells. It belongs to the villin/gelsolin/fragmin superfamily of actin binding proteins and is composed of six gelsolin-homology domains at its core and a villin headpiece domain at its C terminus. Recently, several villin family members from plants have been shown to sever, cap, and bundle actin filaments in vitro. Here, we characterized a villin isovariant, Arabidopsis thaliana VILLIN5 (VLN5), that is highly and preferentially expressed in pollen. VLN5 loss-of-function retarded pollen tube growth and sensitized actin filaments in pollen grains and tubes to latrunculin B. In vitro biochemical analyses revealed that VLN5 is a typical member of the villin family and retains a full suite of activities, including barbed-end capping, filament bundling, and calcium-dependent severing. The severing activity was confirmed with time-lapse evanescent wave microscopy of individual actin filaments in vitro. We propose that VLN5 is a major regulator of actin filament stability and turnover that functions in concert with oscillatory calcium gradients in pollen and therefore plays an integral role in pollen germination and tube growth.
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