The DOI matches its Crossref record; 36 of the 36 references it cites were found in a registry or an index.
The molecular architecture of lamins in somatic cells
Open accessAbstract
The nuclear lamina is a fundamental constituent of metazoan nuclei. It is composed mainly of lamins, which are intermediate filament proteins that assemble into a filamentous meshwork, bridging the nuclear envelope and chromatin. Besides providing structural stability to the nucleus, the lamina is involved in many nuclear activities, including chromatin organization, transcription and replication. However, the structural organization of the nuclear lamina is poorly understood. Here we use cryo-electron tomography to obtain a detailed view of the organization of the lamin meshwork within the lamina. Data analysis of individual lamin filaments resolves a globular-decorated fibre appearance and shows that A- and B-type lamins assemble into tetrameric filaments of 3.5 nm thickness. Thus, lamins exhibit a structure that is remarkably different from the other canonical cytoskeletal elements. Our findings define the architecture of the nuclear lamin meshworks at molecular resolution, providing insights into their role in scaffolding the nuclear lamina.
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UCSF Chimera—A visualization system for exploratory research and analysis
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Lamin A/C deficiency causes defective nuclear mechanics and mechanotransduction
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The nuclear lamina is a meshwork of intermediate-type filaments
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Nuclear Lamins: Their Structure, Assembly, and Interactions
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Intermediate filaments: from cell architecture to nanomechanics
Herrmann, H., Bär, H., Kreplak, L., Strelkov, S. V., & Aebi, U. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2197 · Cited by 698
Nuclear Lamins: Laminopathies and Their Role in Premature Ageing
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Visualizing the molecular sociology at the HeLa cell nuclear periphery
Mahamid, J., Pfeffer, S., Schaffer, M., Villa, E., Danev, R., Kuhn Cuellar, L., Förster, F., Hyman, A. A., Plitzko, J. M., & Baumeister, W. (2016) · Science · doi:10.1126/science.aad8857 · Cited by 576
The nuclear lamins: flexibility in function
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Cited by
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
Molecular pathology of laminopathies
Shin, J.-Y., & Worman, H. J. (2022) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev-pathol-042220-034240 · Cited by 130
Vimentin filaments integrate low-complexity domains in a complex helical structure
Eibauer, M., Weber, M. S., Kronenberg-Tenga, R., Beales, C. T., Boujemaa-Paterski, R., Turgay, Y., Sivagurunathan, S., Kraxner, J., Köster, S., Goldman, R. D., et al. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-024-01261-2 · Cited by 87
Self-citationSpatial chromatin organization and gene regulation at the nuclear lamina
Guerreiro, I., & Kind, J. (2019) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2019.04.008 · Cited by 59
Nuclear Mechanotransduction in Skeletal Muscle
Jabre, S., Hleihel, W., & Coirault, C. (2021) · Cells · doi:10.3390/cells10020318 · Cited by 31
Metadata
- Authors
- Turgay, Y., Eibauer, M., Goldman, A. E., Shimi, T., Khayat, M., Ben-Harush, K., Dubrovsky-Gaupp, A., Sapra, K. T., Goldman, R. D., & Medalia, O.
- Venue
- Nature
- Published
- 2017-03
- Volume
- 543
- Issue
- 7644
- Pages
- 261-264
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2593053801
- Cited by
- 423
- References
- 36
- FWCI
- 17.66
- Type
- journal article
- Language
- en
- Open access
- green
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- Turgay, Y., Eibauer, M., Goldman, A. E., Shimi, T., Khayat, M., Ben-Harush, K., Dubrovsky-Gaupp, A., Sapra, K. T., Goldman, R. D., & Medalia, O. (2017). The molecular architecture of lamins in somatic cells. Nature. https://doi.org/10.1038/nature21382
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