ArticleProceedings of the National Academy of Sciences of the United States of America2022
Nuclear lamin isoforms differentially contribute to LINC complex-dependent nucleocytoskeletal coupling and whole-cell mechanics.
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 72 papers.
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Who cites it
72 citing papers in PubMed, 92 citations in OpenAlex.
- The nucleus as a mechanobiological hub in muscle aging.Nucleus (Austin, Tex.) · 2026Review
- In vivo DNA damage protection during cell migration across confining embryonic tissue environments.Nature cell biology · 2026Article
- Mechanical regulation of cell memory.Nature structural & molecular biology · 2026Review
- Proteostasis of organelles in aging and disease.The FEBS journal · 2026Review
- Epistemological parameters in the recent era of nuclear organization and function.Molecular biology of the cell · 2026Review
- Navigating the cancer cell nucleus: lamins at the interface of epigenetic regulation and tumorigenesis.Molecular biology reports · 2026Review
- The p.R249W Mutation inCells · 2026Article
- Multiscale Architecture and Mechanics of the Cell Nucleus: Implications for Disease, Bioengineering and Nanomedicine.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Review
- Myocardial mechanics displaying on visual structural color hydrogel microcolumn arrays.Journal of nanobiotechnology · 2026Article
- Changes in nuclear and actin mechanics from G1 to G2 affect nuclear integrity.Journal of cell science · 2026Article
- Getting nuclear size just right - emerging mechanisms regulating nuclear scaling and morphology.Journal of cell science · 2026Review
- Review
- Vimentin molecular linkages with nesprin-3 enhance nuclear deformations by cell geometric constraints.Scientific reports · 2026Article
- Microcephaly-associated genes asp and Sas4 influence chromatin organization and nuclear lamina structure in Drosophila melanogaster.Development (Cambridge, England) · 2026Article
- Matrix stiffness induces midnolin-dependent lamin B1 degradation to control myoblast differentiation.EMBO reports · 2026Article
- Stiffness-dependent alveolar type II cell senescence in idiopathic pulmonary fibrosis.Cell communication and signaling : CCS · 2026Article
- Mechanical-biochemical signaling accelerates scleral remodeling in myopia via the LaminA/C-Emerin-MKL1 axis.Cell communication and signaling : CCS · 2026Article
- Nuclear Lamins: A Molecular Bridge Coupling Extracellular Mechanical Cues to Intranuclear Signal Transduction and Gene Regulation.International journal of molecular sciences · 2026Review
- Dynamic changes in Lamin B1 and heterochromatin coincide with chromatin condensation during human erythropoiesis.Genome biology · 2026Article
- Nuclear blebs are composed of variable chromatin states but consistently enrich transcription initiation relative to elongation.bioRxiv : the preprint server for biology · 2026Article
12 more citing papers are in PubMed but not listed here.
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Authors and funding
16 authors at 9 institutions in 2 countries.
Funding
Abstract
The ability of a cell to regulate its mechanical properties is central to its function. Emerging evidence suggests that interactions between the cell nucleus and cytoskeleton influence cell mechanics through poorly understood mechanisms. Here we conduct quantitative confocal imaging to show that the loss of A-type lamins tends to increase nuclear and cellular volume while the loss of B-type lamins behaves in the opposite manner. We use fluorescence recovery after photobleaching, atomic force microscopy, optical tweezer microrheology, and traction force microscopy to demonstrate that A-type lamins engage with both F-actin and vimentin intermediate filaments (VIFs) through the linker of nucleoskeleton and cytoskeleton (LINC) complexes to modulate cortical and cytoplasmic stiffness as well as cellular contractility in mouse embryonic fibroblasts (MEFs). In contrast, we show that B-type lamins predominantly interact with VIFs through LINC complexes to regulate cytoplasmic stiffness and contractility. We then propose a physical model mediated by the lamin–LINC complex that explains these distinct mechanical phenotypes (mechanophenotypes). To verify this model, we use dominant negative constructs and RNA interference to disrupt the LINC complexes that facilitate the interaction of the nucleus with the F-actin and VIF cytoskeletons and show that the loss of these elements results in mechanophenotypes like those observed in MEFs that lack A- or B-type lamin isoforms. Finally, we demonstrate that the loss of each lamin isoform softens the cell nucleus and enhances constricted cell migration but in turn increases migration-induced DNA damage. Together, our findings uncover distinctive roles for each of the four major lamin isoforms in maintaining nucleocytoskeletal interactions and cellular mechanics.
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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.