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Trends Cell Biol. 2014 Apr;24(4):247-56. doi: 10.1016/j.tcb.2013.11.004. Epub 2013 Dec 2.

Broken nuclei--lamins, nuclear mechanics, and disease.

Author information

1
Weill Institute for Cell and Molecular Biology, Cornell University, 526 Campus Road, Ithaca, NY 14853, USA.
2
Department of Biomedical Engineering/Weill Institute for Cell and Molecular Biology, Cornell University, 526 Campus Road, Ithaca, NY 14853, USA. Electronic address: jan.lammerding@cornell.edu.

Abstract

Mutations in lamins, which are ubiquitous nuclear intermediate filaments, lead to a variety of disorders including muscular dystrophy and dilated cardiomyopathy. Lamins provide nuclear stability, help connect the nucleus to the cytoskeleton, and can modulate chromatin organization and gene expression. Nonetheless, the diverse functions of lamins remain incompletely understood. We focus here on the role of lamins on nuclear mechanics and their involvement in human diseases. Recent findings suggest that lamin mutations can decrease nuclear stability, increase nuclear fragility, and disturb mechanotransduction signaling, possibly explaining the muscle-specific defects in many laminopathies. At the same time, altered lamin expression has been reported in many cancers, where the resulting increased nuclear deformability could enhance the ability of cells to transit tight interstitial spaces, thereby promoting metastasis.

KEYWORDS:

cell mechanics; cytoskeleton; gene regulation; laminopathy; protein assembly/structure

PMID:
24309562
PMCID:
PMC3972295
DOI:
10.1016/j.tcb.2013.11.004
[Indexed for MEDLINE]
Free PMC Article

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