Structural organization of nuclear lamins A, C, B1, and B2 revealed by superresolution microscopy

Takeshi Shimia, Mark Kittisopikul, Joseph Tran, Anne E. Goldman, Stephen A. Adam, Yixian Zheng, Khuloud Jaqaman, Robert D. Goldman

Research output: Contribution to journalArticle

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Abstract

The nuclear lamina is a key structural element of the metazoan nucleus. However, the structural organization of the major proteins composing the lamina is poorly defined. Using three-dimensional structured illumination microscopy and computational image analysis, we characterized the supramolecular structures of lamin A, C, B1, and B2 in mouse embryo fibroblast nuclei. Each isoform forms a distinct fiber meshwork, with comparable physical characteristics with respect to mesh edge length, mesh face area and shape, and edge connectivity to form faces. Some differences were found in face areas among isoforms due to variation in the edge lengths and number of edges per face, suggesting that each meshwork has somewhat unique assembly characteristics. In fibroblasts null for the expression of either lamins A/C or lamin B1, the remaining lamin meshworks are altered compared with the lamin meshworks in wild-type nuclei or nuclei lacking lamin B2. Nuclei lacking LA/C exhibit slightly enlarged meshwork faces and some shape changes, whereas LB1-deficient nuclei exhibit primarily a substantial increase in face area. These studies demonstrate that individual lamin isoforms assemble into complex networks within the nuclear lamina and that A-and B-type lamins have distinct roles in maintaining the organization of the nuclear lamina.

Original languageEnglish (US)
Pages (from-to)4075-4086
Number of pages12
JournalMolecular Biology of the Cell
Volume26
Issue number22
DOIs
StatePublished - Nov 5 2015

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Nuclear Lamina
Lamins
Lamin Type A
Microscopy
Protein Isoforms
Fibroblasts
Lamin Type B
Lighting
Embryonic Structures
Proteins

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

Cite this

Shimia, T., Kittisopikul, M., Tran, J., Goldman, A. E., Adam, S. A., Zheng, Y., ... Goldman, R. D. (2015). Structural organization of nuclear lamins A, C, B1, and B2 revealed by superresolution microscopy. Molecular Biology of the Cell, 26(22), 4075-4086. https://doi.org/10.1091/mbc.E15-07-0461

Structural organization of nuclear lamins A, C, B1, and B2 revealed by superresolution microscopy. / Shimia, Takeshi; Kittisopikul, Mark; Tran, Joseph; Goldman, Anne E.; Adam, Stephen A.; Zheng, Yixian; Jaqaman, Khuloud; Goldman, Robert D.

In: Molecular Biology of the Cell, Vol. 26, No. 22, 05.11.2015, p. 4075-4086.

Research output: Contribution to journalArticle

Shimia, T, Kittisopikul, M, Tran, J, Goldman, AE, Adam, SA, Zheng, Y, Jaqaman, K & Goldman, RD 2015, 'Structural organization of nuclear lamins A, C, B1, and B2 revealed by superresolution microscopy', Molecular Biology of the Cell, vol. 26, no. 22, pp. 4075-4086. https://doi.org/10.1091/mbc.E15-07-0461
Shimia, Takeshi ; Kittisopikul, Mark ; Tran, Joseph ; Goldman, Anne E. ; Adam, Stephen A. ; Zheng, Yixian ; Jaqaman, Khuloud ; Goldman, Robert D. / Structural organization of nuclear lamins A, C, B1, and B2 revealed by superresolution microscopy. In: Molecular Biology of the Cell. 2015 ; Vol. 26, No. 22. pp. 4075-4086.
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