The nuclear lamina comes of age

Yosef Gruenbaum; Ayelet Margalit; Robert D. Goldman; Dale K. Shumaker; Katherine L. Wilson

doi:10.1038/nrm1550

The nuclear lamina comes of age

Yosef Gruenbaum^*, Ayelet Margalit, Robert D. Goldman, Dale K. Shumaker, Katherine L. Wilson

^*Corresponding author for this work

Research output: Contribution to journal › Review article › peer-review

716 Scopus citations

Abstract

Many nuclear proteins form lamin-dependent complexes, including LEM-domain proteins, nesprins and SUN-domain proteins. These complexes have roles in chromatin organization, gene regulation and signal transduction. Some link the nucleoskeleton to cytoskeletal structures, ensuring that the nucleus and centrosome assume appropriate intracellular positions. These complexes provide new insights into cell architecture, as well as a foundation for the understanding of the molecular mechanisms that underlie the human laminopathies - clinical disorders that range from Emery-Dreifuss muscular dystrophy to the accelerated ageing seen in Hutchinson-Gilford progeria syndrome.

Original language	English (US)
Pages (from-to)	21-31
Number of pages	11
Journal	Nature Reviews Molecular Cell Biology
Volume	6
Issue number	1
DOIs	https://doi.org/10.1038/nrm1550
State	Published - Jan 2005

Funding

We thank A. Fainsod, P. Collas, M. Taira, H. Worman, J. Holaska and M. Mansharamani for comments. We apologize to authors whose work was not cited directly due to space limitations. We gratefully acknowledge support from the Israel Science Foundation and the German Cancer Research Center to Y.G., and the National Institutes of Health to K.L.W.

ASJC Scopus subject areas

Molecular Biology
Cell Biology

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title = "The nuclear lamina comes of age",

abstract = "Many nuclear proteins form lamin-dependent complexes, including LEM-domain proteins, nesprins and SUN-domain proteins. These complexes have roles in chromatin organization, gene regulation and signal transduction. Some link the nucleoskeleton to cytoskeletal structures, ensuring that the nucleus and centrosome assume appropriate intracellular positions. These complexes provide new insights into cell architecture, as well as a foundation for the understanding of the molecular mechanisms that underlie the human laminopathies - clinical disorders that range from Emery-Dreifuss muscular dystrophy to the accelerated ageing seen in Hutchinson-Gilford progeria syndrome.",

author = "Yosef Gruenbaum and Ayelet Margalit and Goldman, {Robert D.} and Shumaker, {Dale K.} and Wilson, {Katherine L.}",

note = "Funding Information: We thank A. Fainsod, P. Collas, M. Taira, H. Worman, J. Holaska and M. Mansharamani for comments. We apologize to authors whose work was not cited directly due to space limitations. We gratefully acknowledge support from the Israel Science Foundation and the German Cancer Research Center to Y.G., and the National Institutes of Health to K.L.W.",

year = "2005",

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doi = "10.1038/nrm1550",

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N1 - Funding Information: We thank A. Fainsod, P. Collas, M. Taira, H. Worman, J. Holaska and M. Mansharamani for comments. We apologize to authors whose work was not cited directly due to space limitations. We gratefully acknowledge support from the Israel Science Foundation and the German Cancer Research Center to Y.G., and the National Institutes of Health to K.L.W.

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N2 - Many nuclear proteins form lamin-dependent complexes, including LEM-domain proteins, nesprins and SUN-domain proteins. These complexes have roles in chromatin organization, gene regulation and signal transduction. Some link the nucleoskeleton to cytoskeletal structures, ensuring that the nucleus and centrosome assume appropriate intracellular positions. These complexes provide new insights into cell architecture, as well as a foundation for the understanding of the molecular mechanisms that underlie the human laminopathies - clinical disorders that range from Emery-Dreifuss muscular dystrophy to the accelerated ageing seen in Hutchinson-Gilford progeria syndrome.

AB - Many nuclear proteins form lamin-dependent complexes, including LEM-domain proteins, nesprins and SUN-domain proteins. These complexes have roles in chromatin organization, gene regulation and signal transduction. Some link the nucleoskeleton to cytoskeletal structures, ensuring that the nucleus and centrosome assume appropriate intracellular positions. These complexes provide new insights into cell architecture, as well as a foundation for the understanding of the molecular mechanisms that underlie the human laminopathies - clinical disorders that range from Emery-Dreifuss muscular dystrophy to the accelerated ageing seen in Hutchinson-Gilford progeria syndrome.

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The nuclear lamina comes of age

Abstract

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