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Nucleus-dependent sarcomere assembly is mediated by the LINC complex
Two defining characteristics of muscle cells are the many precisely positioned nuclei and the linearly arranged sarcomeres, yet the relationship between these two features is not known. We show that nuclear positioning precedes sarcomere formation. Furthermore, ZASP-GFP, a Z-line protein, colocalize...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4966977/ https://www.ncbi.nlm.nih.gov/pubmed/27307582 http://dx.doi.org/10.1091/mbc.E16-01-0021 |
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author | Auld, Alexander L. Folker, Eric S. |
author_facet | Auld, Alexander L. Folker, Eric S. |
author_sort | Auld, Alexander L. |
collection | PubMed |
description | Two defining characteristics of muscle cells are the many precisely positioned nuclei and the linearly arranged sarcomeres, yet the relationship between these two features is not known. We show that nuclear positioning precedes sarcomere formation. Furthermore, ZASP-GFP, a Z-line protein, colocalizes with F-actin in puncta at the cytoplasmic face of nuclei before sarcomere assembly. In embryos with mispositioned nuclei, ZASP-GFP is still recruited to the nuclei before its incorporation into sarcomeres. Furthermore, the first sarcomeres appear in positions close to the nuclei, regardless of nuclear position. These data suggest that the interaction between sarcomere proteins and nuclei is not dependent on properly positioned nuclei. Mechanistically, ZASP-GFP localization to the cytoplasmic face of the nucleus did require the linker of nucleoskeleton and cytoskeleton (LINC) complex. Muscle-specific depletion of klarsicht (nesprin) or klariod (SUN) blocked the recruitment of ZASP-GFP to the nucleus during the early stages of sarcomere assembly. As a result, sarcomeres were poorly formed and the general myofibril network was less stable, incomplete, and/or torn. These data suggest that the nucleus, through the LINC complex, is crucial for the proper assembly and stability of the sarcomere network. |
format | Online Article Text |
id | pubmed-4966977 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-49669772016-10-16 Nucleus-dependent sarcomere assembly is mediated by the LINC complex Auld, Alexander L. Folker, Eric S. Mol Biol Cell Brief Reports Two defining characteristics of muscle cells are the many precisely positioned nuclei and the linearly arranged sarcomeres, yet the relationship between these two features is not known. We show that nuclear positioning precedes sarcomere formation. Furthermore, ZASP-GFP, a Z-line protein, colocalizes with F-actin in puncta at the cytoplasmic face of nuclei before sarcomere assembly. In embryos with mispositioned nuclei, ZASP-GFP is still recruited to the nuclei before its incorporation into sarcomeres. Furthermore, the first sarcomeres appear in positions close to the nuclei, regardless of nuclear position. These data suggest that the interaction between sarcomere proteins and nuclei is not dependent on properly positioned nuclei. Mechanistically, ZASP-GFP localization to the cytoplasmic face of the nucleus did require the linker of nucleoskeleton and cytoskeleton (LINC) complex. Muscle-specific depletion of klarsicht (nesprin) or klariod (SUN) blocked the recruitment of ZASP-GFP to the nucleus during the early stages of sarcomere assembly. As a result, sarcomeres were poorly formed and the general myofibril network was less stable, incomplete, and/or torn. These data suggest that the nucleus, through the LINC complex, is crucial for the proper assembly and stability of the sarcomere network. The American Society for Cell Biology 2016-08-01 /pmc/articles/PMC4966977/ /pubmed/27307582 http://dx.doi.org/10.1091/mbc.E16-01-0021 Text en © 2016 Auld and Folker. 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 for Cell Biology. |
spellingShingle | Brief Reports Auld, Alexander L. Folker, Eric S. Nucleus-dependent sarcomere assembly is mediated by the LINC complex |
title | Nucleus-dependent sarcomere assembly is mediated by the LINC complex |
title_full | Nucleus-dependent sarcomere assembly is mediated by the LINC complex |
title_fullStr | Nucleus-dependent sarcomere assembly is mediated by the LINC complex |
title_full_unstemmed | Nucleus-dependent sarcomere assembly is mediated by the LINC complex |
title_short | Nucleus-dependent sarcomere assembly is mediated by the LINC complex |
title_sort | nucleus-dependent sarcomere assembly is mediated by the linc complex |
topic | Brief Reports |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4966977/ https://www.ncbi.nlm.nih.gov/pubmed/27307582 http://dx.doi.org/10.1091/mbc.E16-01-0021 |
work_keys_str_mv | AT auldalexanderl nucleusdependentsarcomereassemblyismediatedbythelinccomplex AT folkererics nucleusdependentsarcomereassemblyismediatedbythelinccomplex |