ArticleThe Journal of cell biology2020
Nesprins are mechanotransducers that discriminate epithelial-mesenchymal transition programs.
Article in The Journal of cell biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 57 citations in OpenAlex.
- Nuclear mechanotransduction: tools for mechanical perturbation and chromatin characterization.Nucleus (Austin, Tex.) · 2026Review
- Maintaining Genome Integrity: Actin Polymerization Stabilizes Chromatin Bridges in Cytokinesis.International journal of molecular sciences · 2026Review
- Molecular tension indicators reveal unexpectedly complex regulation of tension in live mouse organs.Communications biology · 2026Article
- Force-dependent structural dynamics of the giant nesprin-2.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Emerin acts as a mechanosensor linking force transmission and disease.Frontiers in oncology · 2026Review
- The dual guardians of cellular stability: exploring nesprin and lamin in senescence.Cell death & disease · 2025Review
- KASH proteins transform from passive tethers to dynamic conductors of motor-driven nuclear dynamics.Current opinion in cell biology · 2025Review
- Tension-sensitive LINC-RhoA signaling prevents chromatin bridge breakage in cytokinesis.The EMBO journal · 2025Article
- Epigenetic Changes Regulating Epithelial-Mesenchymal Plasticity in Human Trophoblast Differentiation.Cells · 2025Article
- The mechanism of nesprin-2 accumulation at the nucleus front during confined cell migration.Biophysical journal · 2025Article
- Induction of DNA Demethylation: Strategies and Consequences.Epigenomes · 2025Review
- Feeling the force from within - new tools and insights into nuclear mechanotransduction.Journal of cell science · 2025Review
- Nuclear envelope proteins, mechanotransduction, and their contribution to breast cancer progression.npj biological physics and mechanics · 2025Review
- Tutorial: fluorescence lifetime microscopy of membrane mechanosensitive Flipper probes.Nature protocols · 2024Review
- Emerin deficiency drives MCF7 cells to an invasive phenotype.bioRxiv : the preprint server for biology · 2024Article
- Biomaterial-based mechanical regulation facilitates scarless wound healing with functional skin appendage regeneration.Military Medical Research · 2024Review
- From cells to form: A roadmap to study shape emergence in vivo.Biophysical journal · 2023Review
- Disulfide bond in SUN2 regulates dynamic remodeling of LINC complexes at the nuclear envelope.Life science alliance · 2023Article
- Nuclear lamina strain states revealed by intermolecular force biosensor.Nature communications · 2023Article
- The linker of nucleoskeleton and cytoskeleton complex is required for X-ray-induced epithelial-mesenchymal transition.Journal of radiation research · 2023Article
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Authors and funding
10 authors at 5 institutions in 2 countries.
Funding
Abstract
LINC complexes are transmembrane protein assemblies that physically connect the nucleoskeleton and cytoskeleton through the nuclear envelope. Dysfunctions of LINC complexes are associated with pathologies such as cancer and muscular disorders. The mechanical roles of LINC complexes are poorly understood. To address this, we used genetically encoded FRET biosensors of molecular tension in a nesprin protein of the LINC complex of fibroblastic and epithelial cells in culture. We exposed cells to mechanical, genetic, and pharmacological perturbations, mimicking a range of physiological and pathological situations. We show that nesprin experiences tension generated by the cytoskeleton and acts as a mechanical sensor of cell packing. Moreover, nesprin discriminates between inductions of partial and complete epithelial-mesenchymal transitions. We identify the implicated mechanisms, which involve α-catenin capture at the nuclear envelope by nesprin upon its relaxation, thereby regulating β-catenin transcription. Our data thus implicate LINC complex proteins as mechanotransducers that fine-tune β-catenin signaling in a manner dependent on the epithelial-mesenchymal transition program.
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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.