ArticleBiophysical journal2011
The LIM domain of zyxin is sufficient for force-induced accumulation of zyxin during cell migration.
Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
45 citing papers in PubMed, 62 citations in OpenAlex.
- Reconstituted nascent adhesion condensates drive actin polymerization on supported lipid bilayers.Science advances · 2026Article
- The Potential Link and Role of Zyxin in the Pathogenesis of Psoriasis and Its Associated Comorbidities.International journal of molecular sciences · 2026Article
- The mechanosensitive channel ELKIN1 regulates cellular adaptations to simulated microgravity.NPJ microgravity · 2025Article
- Tandem LIM domain-containing proteins, LIMK1 and LMO1, directly bind to force-bearing keratin intermediate filaments.Cell reports · 2024Article
- Zyxin is important for the stability and function of podocytes, especially during mechanical stretch.Communications biology · 2024Article
- IOP and glaucoma damage: The essential role of optic nerve head and retinal mechanosensors.Progress in retinal and eye research · 2024Review
- From stress fiber to focal adhesion: a role of actin crosslinkers in force transmission.Frontiers in cell and developmental biology · 2024Review
- The role of zyxin in signal transduction and its relationship with diseases.Frontiers in molecular biosciences · 2024Review
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- Article
- Working a second job: Cell adhesion proteins that moonlight in the nucleus.Frontiers in cell and developmental biology · 2023Review
- Contribution of mechanical homeostasis to epithelial-mesenchymal transition.Cellular oncology (Dordrecht, Netherlands) · 2022Review
- Expression of the phagocytic receptors αFrontiers in immunology · 2022Article
- A Layered View on Focal Adhesions.Biology · 2021Review
- LIM domain proteins in cell mechanobiology.Cytoskeleton (Hoboken, N.J.) · 2021Review
- Manipulation of Focal Adhesion Signaling by Pathogenic Microbes.International journal of molecular sciences · 2021Review
- Mechanosensing through Direct Binding of Tensed F-Actin by LIM Domains.Developmental cell · 2020Article
- Genetic analysis of the molecular regulation of electric fields-guided glia migration.Scientific reports · 2020Article
- The Intersection of Mechanotransduction and Regenerative Osteogenic Materials.Advanced healthcare materials · 2020Review
- Tissue transglutaminase 2 regulates tumor cell tensional homeostasis by increasing contractility.Journal of cell science · 2020Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Cellular responses to mechanical perturbation are vital to cell physiology. In particular, migrating cells have been shown to sense substrate stiffness and alter cell morphology and speed. Zyxin is a focal adhesion protein that responds to external mechanical forces; however, the mechanisms of zyxin recruitment at force-bearing sites are unknown. Using force-sensing microfabricated substrates, we simultaneously measured traction force and zyxin recruitment at force-bearing sites. GFP-tagged zyxin accumulates at force-bearing sites at the leading edge, but not at the trailing edge, of migrating epithelial cells. Zyxin recruitment at force-bearing sites depends on Rho-kinase and myosin II activation, suggesting that zyxin responds not only to the externally applied force, as previously shown, but also to the internally generated actin-myosin force. Zyxin in turn recruits vasodilator-stimulated phosphoprotein, a regulator of actin assembly, to force-bearing sites. To dissect the domains of zyxin that are essential for this unique force-dependent accumulation, we generated two zyxin truncation mutants: one lacking the LIM domain (ΔLIM) and one containing only the LIM domain with all three LIM motifs (LIM). GFP-tagged ΔLIM does not localize to the force-bearing sites, but GFP-tagged zyxin LIM-domain is sufficient for the recruitment to and dynamics at force-bearing focal adhesions. Furthermore, one or two LIM motifs are not sufficient for force-dependent accumulation, suggesting that all three LIM motifs are required. Therefore, the LIM domain of zyxin recruits zyxin to force-bearing sites at the leading edge of migrating cells.
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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.