ArticleProceedings of the National Academy of Sciences of the United States of America2022
Structural mechanism for bidirectional actin cross-linking by T-plastin.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 29 citations in OpenAlex.
- In silico conformational dynamics of the α-actinin-2 actin-binding domain upon phosphorylation.Biophysical journal · 2026Article
- Article
- Loss of cyclase-associated protein 2 alters actin cytoskeleton organization and biomechanical properties of the ocular lens.Journal of cell science · 2026Article
- The Role of Plastin in Bone, Cartilage, and Related Diseases.Calcified tissue international · 2026Review
- Force-modulated structural landscape of the catch bonding F-actin crosslinker α-actinin-4.bioRxiv : the preprint server for biology · 2026Article
- Pathogenic mechanism of the PLS1 gene variant in hearing loss and functional validation in a zebrafish model.Scientific reports · 2026Article
- Germ line LCP1 mutations cause immunodeficiency with neutropenia, monocytopenia, lymphopenia, and defective cytokinesis.Blood advances · 2026Article
- Actin isoform-specific interactions revealed byProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Genetic Diagnosis and Clinical Features of Fetuses With Congenital Diaphragmatic Hernia.Prenatal diagnosis · 2025Article
- Human Plastins are Novel Cytoskeletal pH Sensors with a Reduced F-actin Bundling Capacity at Basic pH.Journal of molecular biology · 2025Article
- Structure of the Huntingtin F-actin complex reveals its role in cytoskeleton organization.Science advances · 2025Article
- Shaping epithelial tissues by stem cell mechanics in development and cancer.Nature reviews. Molecular cell biology · 2025Review
- Fascin structural plasticity mediates flexible actin bundle construction.Nature structural & molecular biology · 2025Article
- Role of LMO7 in cancer (Review).Oncology reports · 2024Review
- Myosin forces elicit an F-actin structural landscape that mediates mechanosensitive protein recognition.bioRxiv : the preprint server for biology · 2024Article
- Stabilization of F-actin by Salmonella effector SipA resembles the structural effects of inorganic phosphate and phalloidin.Structure (London, England : 1993) · 2024Article
- Fascin structural plasticity mediates flexible actin bundle construction.bioRxiv : the preprint server for biology · 2024Article
- Stabilization of F-actin bybioRxiv : the preprint server for biology · 2023Article
- Structural basis for subversion of host cell actin cytoskeleton duringScience advances · 2023Article
- Cardiomyocyte external mechanical unloading activates modifications of α-actinin differently from sarcomere-originated unloading.The FEBS journal · 2023Article
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 1 country.
Funding
Abstract
To orchestrate cell mechanics, trafficking, and motility, cytoskeletal filaments must assemble into higher-order networks whose local subcellular architecture and composition specify their functions. Cross-linking proteins bridge filaments at the nanoscale to control a network's μm-scale geometry, thereby conferring its mechanical properties and functional dynamics. While these interfilament linkages are key determinants of cytoskeletal function, their structural mechanisms remain poorly understood. Plastins/fimbrins are an evolutionarily ancient family of tandem calponin-homology domain (CHD) proteins required to construct multiple classes of actin networks, which feature diverse geometries specialized to power cytokinesis, microvilli and stereocilia biogenesis, and persistent cell migration. Here, we focus on the structural basis of actin network assembly by human T-plastin, a ubiquitously expressed isoform necessary for the maintenance of stable cellular protrusions generated by actin polymerization forces. By implementing a machine-learning-enabled cryo-electron microscopy pipeline for visualizing cross-linkers bridging multiple filaments, we uncover a sequential bundling mechanism enabling T-plastin to bridge pairs of actin filaments in both parallel and antiparallel orientations. T-plastin populates distinct structural landscapes in these two bridging orientations that are selectively compatible with actin networks featuring divergent architectures and functions. Our structural, biochemical, and cell biological data highlight inter-CHD linkers as key structural elements underlying flexible but stable cross-linking that are likely to be disrupted by T-plastin mutations that cause hereditary bone diseases.
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Registered trials
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.