ArticleCellular and molecular life sciences : CMLS2012
Nesprin interchain associations control nuclear size.
Article in Cellular and molecular life sciences : CMLS, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
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Who cites it
58 citing papers in PubMed.
- Nuclear mechanobiology: a brief history and five unresolved questions.Nucleus (Austin, Tex.) · 2026Article
- Article
- A Novel Emerin/Nesprin-3 Interaction Mediates Nuclear Size Changes Induced by Oncogenic KRAS in Pancreatic Cancer Cells.Molecular and cellular biology · 2026Article
- Nuclear Mechanotransduction at the Crossroads: How Membrane Receptors Remodel the Perinuclear Cytoskeleton to Drive Cancer and Disease.International journal of biological sciences · 2026Review
- The dual guardians of cellular stability: exploring nesprin and lamin in senescence.Cell death & disease · 2025Review
- Cancer-associated SPOP mutations enlarge nuclear size and facilitate nuclear envelope rupture upon farnesyltransferase inhibitor treatment.The Journal of clinical investigation · 2025Article
- Calpain-1 weakens the nuclear envelope and promotes the release of neutrophil extracellular traps.Cell communication and signaling : CCS · 2024Article
- Nesprin-1: novel regulator of striated muscle nuclear positioning and mechanotransduction.Biochemical Society transactions · 2023Review
- Article
- Review
- Article
- Nucleus size and its effect on nucleosome stability in living cells.Biophysical journal · 2022Article
- LINCing Senescence and Nuclear Envelope Changes.Cells · 2022Review
- Chemical Interrogation of Nuclear Size Identifies Compounds with Cancer Cell Line-Specific Effects on Migration and Invasion.ACS chemical biology · 2022Article
- A Multisensory Network Drives Nuclear Mechanoadaptation.Biomolecules · 2022Review
- Nuclear Morphological Abnormalities in Cancer: A Search for Unifying Mechanisms.Results and problems in cell differentiation · 2022Article
- Nuclear size rectification: A potential new therapeutic approach to reduce metastasis in cancer.Frontiers in cell and developmental biology · 2022Review
- Nuclear deformation guides chromatin reorganization in cardiac development and disease.Nature biomedical engineering · 2021Article
- Review
- BiallelicGenes · 2021Article
Corrections and comments
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Authors and funding
13 authors.
Funding
Abstract
Nesprins-1/-2/-3/-4 are nuclear envelope proteins, which connect nuclei to the cytoskeleton. The largest nesprin-1/-2 isoforms (termed giant) tether F-actin through their N-terminal actin binding domain (ABD). Nesprin-3, however, lacks an ABD and associates instead to plectin, which binds intermediate filaments. Nesprins are integrated into the outer nuclear membrane via their C-terminal KASH-domain. Here, we show that nesprin-1/-2 ABDs physically and functionally interact with nesprin-3. Thus, both ends of nesprin-1/-2 giant are integrated at the nuclear surface: via the C-terminal KASH-domain and the N-terminal ABD-nesprin-3 association. Interestingly, nesprin-2 ABD or KASH-domain overexpression leads to increased nuclear areas. Conversely, nesprin-2 mini (contains the ABD and KASH-domain but lacks the massive nesprin-2 giant rod segment) expression yields smaller nuclei. Nuclear shrinkage is further enhanced upon nesprin-3 co-expression or microfilament depolymerization. Our findings suggest that multivariate intermolecular nesprin interactions with the cytoskeleton form a lattice-like filamentous network covering the outer nuclear membrane, which determines nuclear size.
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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.