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A laminopathic mutation disrupting lamin filament assembly causes disease-like phenotypes in Caenorhabditis elegans
Mutations in the human LMNA gene underlie many laminopathic diseases, including Emery-Dreifuss muscular dystrophy (EDMD); however, a mechanistic link between the effect of mutations on lamin filament assembly and disease phenotypes has not been established. We studied the ΔK46 Caenorhabditis elegans...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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The American Society for Cell Biology
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3145547/ https://www.ncbi.nlm.nih.gov/pubmed/21653823 http://dx.doi.org/10.1091/mbc.E11-01-0064 |
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author | Bank, Erin M. Ben-Harush, Kfir Wiesel-Motiuk, Naama Barkan, Rachel Feinstein, Naomi Lotan, Oren Medalia, Ohad Gruenbaum, Yosef |
author_facet | Bank, Erin M. Ben-Harush, Kfir Wiesel-Motiuk, Naama Barkan, Rachel Feinstein, Naomi Lotan, Oren Medalia, Ohad Gruenbaum, Yosef |
author_sort | Bank, Erin M. |
collection | PubMed |
description | Mutations in the human LMNA gene underlie many laminopathic diseases, including Emery-Dreifuss muscular dystrophy (EDMD); however, a mechanistic link between the effect of mutations on lamin filament assembly and disease phenotypes has not been established. We studied the ΔK46 Caenorhabditis elegans lamin mutant, corresponding to EDMD-linked ΔK32 in human lamins A and C. Cryo-electron tomography of lamin ΔK46 filaments in vitro revealed alterations in the lateral assembly of dimeric head-to-tail polymers, which causes abnormal organization of tetrameric protofilaments. Green fluorescent protein (GFP):ΔK46 lamin expressed in C. elegans was found in nuclear aggregates in postembryonic stages along with LEM-2. GFP:ΔK46 also caused mislocalization of emerin away from the nuclear periphery, consistent with a decreased ability of purified emerin to associate with lamin ΔK46 filaments in vitro. GFP:ΔK46 animals had motility defects and muscle structure abnormalities. These results show that changes in lamin filament structure can translate into disease-like phenotypes via altering the localization of nuclear lamina proteins, and suggest a model for how the ΔK32 lamin mutation may cause EDMD in humans. |
format | Online Article Text |
id | pubmed-3145547 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-31455472011-10-16 A laminopathic mutation disrupting lamin filament assembly causes disease-like phenotypes in Caenorhabditis elegans Bank, Erin M. Ben-Harush, Kfir Wiesel-Motiuk, Naama Barkan, Rachel Feinstein, Naomi Lotan, Oren Medalia, Ohad Gruenbaum, Yosef Mol Biol Cell Articles Mutations in the human LMNA gene underlie many laminopathic diseases, including Emery-Dreifuss muscular dystrophy (EDMD); however, a mechanistic link between the effect of mutations on lamin filament assembly and disease phenotypes has not been established. We studied the ΔK46 Caenorhabditis elegans lamin mutant, corresponding to EDMD-linked ΔK32 in human lamins A and C. Cryo-electron tomography of lamin ΔK46 filaments in vitro revealed alterations in the lateral assembly of dimeric head-to-tail polymers, which causes abnormal organization of tetrameric protofilaments. Green fluorescent protein (GFP):ΔK46 lamin expressed in C. elegans was found in nuclear aggregates in postembryonic stages along with LEM-2. GFP:ΔK46 also caused mislocalization of emerin away from the nuclear periphery, consistent with a decreased ability of purified emerin to associate with lamin ΔK46 filaments in vitro. GFP:ΔK46 animals had motility defects and muscle structure abnormalities. These results show that changes in lamin filament structure can translate into disease-like phenotypes via altering the localization of nuclear lamina proteins, and suggest a model for how the ΔK32 lamin mutation may cause EDMD in humans. The American Society for Cell Biology 2011-08-01 /pmc/articles/PMC3145547/ /pubmed/21653823 http://dx.doi.org/10.1091/mbc.E11-01-0064 Text en © 2011 Bank et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society of Cell Biology. |
spellingShingle | Articles Bank, Erin M. Ben-Harush, Kfir Wiesel-Motiuk, Naama Barkan, Rachel Feinstein, Naomi Lotan, Oren Medalia, Ohad Gruenbaum, Yosef A laminopathic mutation disrupting lamin filament assembly causes disease-like phenotypes in Caenorhabditis elegans |
title | A laminopathic mutation disrupting lamin filament assembly causes disease-like phenotypes in Caenorhabditis elegans |
title_full | A laminopathic mutation disrupting lamin filament assembly causes disease-like phenotypes in Caenorhabditis elegans |
title_fullStr | A laminopathic mutation disrupting lamin filament assembly causes disease-like phenotypes in Caenorhabditis elegans |
title_full_unstemmed | A laminopathic mutation disrupting lamin filament assembly causes disease-like phenotypes in Caenorhabditis elegans |
title_short | A laminopathic mutation disrupting lamin filament assembly causes disease-like phenotypes in Caenorhabditis elegans |
title_sort | laminopathic mutation disrupting lamin filament assembly causes disease-like phenotypes in caenorhabditis elegans |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3145547/ https://www.ncbi.nlm.nih.gov/pubmed/21653823 http://dx.doi.org/10.1091/mbc.E11-01-0064 |
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