ArticleProceedings of the National Academy of Sciences of the United States of America2009
Rapid formin-mediated actin-filament elongation is essential for polarized plant cell growth.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers.
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Who cites it
87 citing papers in PubMed, 171 citations in OpenAlex.
- Article
- Genome-wide identification and gene expression analysis of Formin homology 2 (FH2) genes in peanut.BMC plant biology · 2026Article
- A High-Thousand-Seed-Weight Mutant ofInternational journal of molecular sciences · 2026Article
- Novel small molecules disrupting polarized cell expansion and development in the moss,Plant biotechnology (Tokyo, Japan) · 2025Article
- Article
- Regulation of cytoskeleton dynamics and its interplay with force in plant cells.Biophysics reviews · 2024Review
- Transmembrane formins as active cargoes of membrane trafficking.Journal of experimental botany · 2024Review
- Regulation of developmental gatekeeping and cell fate transition by the calpain protease DEK1 in Physcomitrium patens.Communications biology · 2024Article
- Cooperative actin filament nucleation by the Arp2/3 complex and formins maintains the homeostatic cortical array in Arabidopsis epidermal cells.The Plant cell · 2024Article
- Genome-Wide Studies ofPlants (Basel, Switzerland) · 2024Article
- Assembly and annotation of the black spruce genome provide insights on spruce phylogeny and evolution of stress response.G3 (Bethesda, Md.) · 2023Article
- Automatic extraction of actin networks in plants.PLoS computational biology · 2023Article
- Cellulose synthase-like D movement in the plasma membrane requires enzymatic activity.The Journal of cell biology · 2023Article
- Armadillo repeat-containing kinesin represents the versatile plus-end-directed transporter in Physcomitrella.Nature plants · 2023Article
- Review
- Actin assembly requirements of the formin Fus1 to build the fusion focus.Journal of cell science · 2022Article
- Cellulose synthesis complexes are homo-oligomeric and hetero-oligomeric in Physcomitrium patens.Plant physiology · 2022Article
- COPII Sec23 proteins form isoform-specific endoplasmic reticulum exit sites with differential effects on polarized growth.The Plant cell · 2022Article
- Cell biology of primary cell wall synthesis in plants.The Plant cell · 2022Review
- The bryophytes Physcomitrium patens and Marchantia polymorpha as model systems for studying evolutionary cell and developmental biology in plants.The Plant cell · 2022Review
27 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Formins are present in all eukaryotes and are essential for the creation of actin-based structures responsible for diverse cellular processes. Because multicellular organisms contain large formin gene families, establishing the physiological functions of formin isoforms has been difficult. Using RNAi, we analyzed the function of all 9 formin genes within the moss Physcomitrella patens. We show that plants lacking class II formins (For2) are severely stunted and composed of spherical cells with disrupted actin organization. In contrast, silencing of all other formins results in normal elongated cell morphology and actin organization. Consistent with a role in polarized growth, For2 are apically localized in growing cells. We show that an N-terminal phosphatase tensin (PTEN)-like domain mediates apical localization. The PTEN-like domain is followed by a conserved formin homology (FH)1-FH2 domain, known to promote actin polymerization. To determine whether apical localization of any FH1-FH2 domain mediates polarized growth, we performed domain swapping. We found that only the class II FH1-FH2, in combination with the PTEN-like domain, rescues polarized growth, because it cannot be replaced with a similar domain from a For1. We used in vitro polymerization assays to dissect the functional differences between these FH1-FH2 domains. We found that both the FH1 and the FH2 domains from For2 are required to mediate exceptionally rapid rates of actin filament elongation, much faster than any other known formin. Thus, our data demonstrate that rapid rates of actin elongation are critical for driving the formation of apical filamentous actin necessary for polarized growth.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.