The DOI matches its Crossref record; 31 of the 31 references it cites were found in a registry or an index.
Lamin A/C and emerin regulate MKL1–SRF activity by modulating actin dynamics
Open accessAbstract
Laminopathies, caused by mutations in the LMNA gene encoding the nuclear envelope proteins lamins A and C, represent a diverse group of diseases that include Emery–Dreifuss muscular dystrophy (EDMD), dilated cardiomyopathy (DCM), limb-girdle muscular dystrophy, and Hutchison–Gilford progeria syndrome. Most LMNA mutations affect skeletal and cardiac muscle by mechanisms that remain incompletely understood. Loss of structural function and altered interaction of mutant lamins with (tissue-specific) transcription factors have been proposed to explain the tissue-specific phenotypes. Here we report in mice that lamin-A/C-deficient (Lmna−/−) and LmnaN195K/N195K mutant cells have impaired nuclear translocation and downstream signalling of the mechanosensitive transcription factor megakaryoblastic leukaemia 1 (MKL1), a myocardin family member that is pivotal in cardiac development and function. Altered nucleo-cytoplasmic shuttling of MKL1 was caused by altered actin dynamics in Lmna−/− and LmnaN195K/N195K mutant cells. Ectopic expression of the nuclear envelope protein emerin, which is mislocalized in Lmna mutant cells and also linked to EDMD and DCM, restored MKL1 nuclear translocation and rescued actin dynamics in mutant cells. These findings present a novel mechanism that could provide insight into the disease aetiology for the cardiac phenotype in many laminopathies, whereby lamin A/C and emerin regulate gene expression through modulation of nuclear and cytoskeletal actin polymerization.
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Cites
Actin dynamics control SRF activity by regulation of its coactivator MAL
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Lamin A/C deficiency causes defective nuclear mechanics and mechanotransduction
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Self-citationLinking actin dynamics and gene transcription to drive cellular motile functions
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Self-citationDefects in nuclear structure and function promote dilated cardiomyopathy in lamin A/C–deficient mice
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Abnormal nuclear shape and impaired mechanotransduction in emerin-deficient cells
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Force triggers YAP nuclear entry by regulating transport across nuclear pores
Elosegui-Artola, A., Andreu, I., Beedle, A. E. M., Lezamiz, A., Uroz, M., Kosmalska, A. J., Oria, R., Kechagia, J. Z., Rico-Lastres, P., Le Roux, A.-L., et al. (2017) · Cell · doi:10.1016/j.cell.2017.10.008 · Cited by 1,491
Mechanics and functional consequences of nuclear deformations
Kalukula, Y., Stephens, A. D., Lammerding, J., & Gabriele, S. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-022-00480-z · Cited by 475
Self-citationNicotinamide Riboside Preserves Cardiac Function in a Mouse Model of Dilated Cardiomyopathy
Diguet, N., Trammell, S. A. J., Tannous, C., Deloux, R., Piquereau, J., Mougenot, N., Gouge, A., Gressette, M., Manoury, B., Blanc, J., et al. (2018) · Circulation · doi:10.1161/circulationaha.116.026099 · Cited by 358
Mechanisms and functions of nuclear envelope remodelling
Ungricht, R., & Kutay, U. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.153 · Cited by 346
MicroRNA-21 preserves the fibrotic mechanical memory of mesenchymal stem cells
Li, C. X., Talele, N. P., Boo, S., Koehler, A., Knee-Walden, E., Balestrini, J. L., Speight, P., Kapus, A., & Hinz, B. (2017) · Nature Materials · doi:10.1038/nmat4780 · Cited by 336
Metadata
- Authors
- Ho, C. Y., Jaalouk, D. E., Vartiainen, M. K., & Lammerding, J.
- Venue
- Nature
- Published
- 2013-05-05
- Volume
- 497
- Issue
- 7450
- Pages
- 507-511
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2119110453
- Cited by
- 455
- References
- 31
- FWCI
- 18.69
- Type
- journal article
- Language
- en
- Open access
- green
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