Abnormal nuclear shape and impaired mechanotransduction in emerin-deficient cells
Emery-Dreifuss muscular dystrophy can be caused by mutations in the nuclear envelope proteins lamin A/C and emerin. We recently demonstrated that A-type lamin-deficient cells have impaired nuclear mechanics and altered mechanotransduction, suggesting two potential disease mechanisms (Lammerding, J.,...
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Published in | The Journal of cell biology Vol. 170; no. 5; pp. 781 - 791 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
United States
Rockefeller University Press
29.08.2005
The Rockefeller University Press |
Subjects | |
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Abstract | Emery-Dreifuss muscular dystrophy can be caused by mutations in the nuclear envelope proteins lamin A/C and emerin. We recently demonstrated that A-type lamin-deficient cells have impaired nuclear mechanics and altered mechanotransduction, suggesting two potential disease mechanisms (Lammerding, J., P.C. Schulze, T. Takahashi, S. Kozlov, T. Sullivan, R.D. Kamm, C.L. Stewart, and R.T. Lee. 2004. J. Clin. Invest. 113:370-378). Here, we examined the function of emerin on nuclear mechanics and strain-induced signaling. Emerin-deficient mouse embryo fibroblasts have abnormal nuclear shape, but in contrast to A-type lamin-deficient cells, exhibit nuclear deformations comparable to wild-type cells in cellular strain experiments, and the integrity of emerin-deficient nuclear envelopes appeared normal in a nuclear microinjection assay. Interestingly, expression of mechanosensitive genes in response to mechanical strain was impaired in emerin-deficient cells, and prolonged mechanical stimulation increased apoptosis in emerin-deficient cells. Thus, emerin-deficient mouse embryo fibroblasts have apparently normal nuclear mechanics but impaired expression of mechanosensitive genes in response to strain, suggesting that emerin mutations may act through altered transcriptional regulation and not by increasing nuclear fragility. |
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AbstractList | Emery-Dreifuss muscular dystrophy can be caused by mutations in the nuclear envelope proteins lamin A/C and emerin. We recently demonstrated that A-type lamin-deficient cells have impaired nuclear mechanics and altered mechanotransduction, suggesting two potential disease mechanisms (Lammerding, J., P.C. Schulze, T. Takahashi, S. Kozlov, T. Sullivan, R.D. Kamm, C.L. Stewart, and R.T. Lee. 2004. J. Clin. Invest. 113:370-378). Here, we examined the function of emerin on nuclear mechanics and strain-induced signaling. Emerin-deficient mouse embryo fibroblasts have abnormal nuclear shape, but in contrast to A-type lamin-deficient cells, exhibit nuclear deformations comparable to wild-type cells in cellular strain experiments, and the integrity of emerin-deficient nuclear envelopes appeared normal in a nuclear microinjection assay. Interestingly, expression of mechanosensitive genes in response to mechanical strain was impaired in emerin-deficient cells, and prolonged mechanical stimulation increased apoptosis in emerin-deficient cells. Thus, emerin-deficient mouse embryo fibroblasts have apparently normal nuclear mechanics but impaired expression of mechanosensitive genes in response to strain, suggesting that emerin mutations may act through altered transcriptional regulation and not by increasing nuclear fragility.[PUBLICATION ABSTRACT] Emery-Dreifuss muscular dystrophy can be caused by mutations in the nuclear envelope proteins lamin A/C and emerin. We recently demonstrated that A-type lamin-deficient cells have impaired nuclear mechanics and altered mechanotransduction, suggesting two potential disease mechanisms (Lammerding, J., P.C. Schulze, T. Takahashi, S. Kozlov, T. Sullivan, R.D. Kamm, C.L. Stewart, and R.T. Lee. 2004. J. Clin. Invest. 113:370–378). Here, we examined the function of emerin on nuclear mechanics and strain-induced signaling. Emerin-deficient mouse embryo fibroblasts have abnormal nuclear shape, but in contrast to A-type lamin-deficient cells, exhibit nuclear deformations comparable to wild-type cells in cellular strain experiments, and the integrity of emerin-deficient nuclear envelopes appeared normal in a nuclear microinjection assay. Interestingly, expression of mechanosensitive genes in response to mechanical strain was impaired in emerin-deficient cells, and prolonged mechanical stimulation increased apoptosis in emerin-deficient cells. Thus, emerin-deficient mouse embryo fibroblasts have apparently normal nuclear mechanics but impaired expression of mechanosensitive genes in response to strain, suggesting that emerin mutations may act through altered transcriptional regulation and not by increasing nuclear fragility. Emery-Dreifuss muscular dystrophy can be caused by mutations in the nuclear envelope proteins lamin A/C and emerin. We recently demonstrated that A-type lamin-deficient cells have impaired nuclear mechanics and altered mechanotransduction, suggesting two potential disease mechanisms (Lammerding, J., P.C. Schulze, T. Takahashi, S. Kozlov, T. Sullivan, R.D. Kamm, C.L. Stewart, and R.T. Lee. 2004. J. Clin. Invest. 113:370-378). Here, we examined the function of emerin on nuclear mechanics and strain-induced signaling. Emerin-deficient mouse embryo fibroblasts have abnormal nuclear shape, but in contrast to A-type lamin-deficient cells, exhibit nuclear deformations comparable to wild-type cells in cellular strain experiments, and the integrity of emerin-deficient nuclear envelopes appeared normal in a nuclear microinjection assay. Interestingly, expression of mechanosensitive genes in response to mechanical strain was impaired in emerin-deficient cells, and prolonged mechanical stimulation increased apoptosis in emerin-deficient cells. Thus, emerin-deficient mouse embryo fibroblasts have apparently normal nuclear mechanics but impaired expression of mechanosensitive genes in response to strain, suggesting that emerin mutations may act through altered transcriptional regulation and not by increasing nuclear fragility. |
Author | Stewart, Colin L Lee, Richard T Hsiao, Janet Kozlov, Serguei Lammerding, Jan Schulze, P. Christian |
AuthorAffiliation | 3 Cancer and Developmental Biology Lab, National Cancer Institute, Frederick, MD 21702 2 HST Division, Massachusetts Institute of Technology, Cambridge, MA 02139 1 Cardiovascular Division, Brigham and Women's Hospital, Boston, MA 02115 |
AuthorAffiliation_xml | – name: 3 Cancer and Developmental Biology Lab, National Cancer Institute, Frederick, MD 21702 – name: 1 Cardiovascular Division, Brigham and Women's Hospital, Boston, MA 02115 – name: 2 HST Division, Massachusetts Institute of Technology, Cambridge, MA 02139 |
Author_xml | – sequence: 1 fullname: Lammerding, Jan – sequence: 2 fullname: Hsiao, Janet – sequence: 3 fullname: Schulze, P. Christian – sequence: 4 fullname: Kozlov, Serguei – sequence: 5 fullname: Stewart, Colin L – sequence: 6 fullname: Lee, Richard T |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/16115958$$D View this record in MEDLINE/PubMed |
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Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Abbreviations used in this paper: BAF, barrier-to-autointegration factor; EDMD, Emery-Dreifuss muscular dystrophy; GAPDH, glyceraldehyde 3-phosphate dehydrogenase; GCL, germ cell-less. Correspondence to Jan Lammerding: jlammerding@rics.bwh.harvard.edu |
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Snippet | Emery-Dreifuss muscular dystrophy can be caused by mutations in the nuclear envelope proteins lamin A/C and emerin. We recently demonstrated that A-type... |
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SubjectTerms | Animals Apoptosis Cell lines Cell nucleus Cell Nucleus - metabolism Cell Nucleus - ultrastructure Cells Cells, Cultured Cellular biology Embryos Fibroblasts Fibroblasts - cytology Fibroblasts - metabolism Fracture mechanics Humans Lamin Type A - genetics Lamin Type A - metabolism Lamins Mechanotransduction, Cellular - physiology Membrane Proteins - genetics Membrane Proteins - metabolism Mice Mice, Knockout Muscular Dystrophy, Emery-Dreifuss - genetics Muscular Dystrophy, Emery-Dreifuss - metabolism Mutation NF-kappa B - metabolism Nuclear membrane Nuclear Proteins Proteins Signal transduction Signal Transduction - physiology Space life sciences Stress, Mechanical Structural strain Thymopoietins - genetics Thymopoietins - metabolism |
Title | Abnormal nuclear shape and impaired mechanotransduction in emerin-deficient cells |
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