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Myomesin is part of an integrity pathway that responds to sarcomere damage and disease
The structure and function of the sarcomere of striated muscle is well studied but the steps of sarcomere assembly and maintenance remain under-characterized. With the aid of chaperones and factors of the protein quality control system, muscle proteins can be folded and assembled into the contractil...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6808450/ https://www.ncbi.nlm.nih.gov/pubmed/31644553 http://dx.doi.org/10.1371/journal.pone.0224206 |
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author | Prill, Kendal Carlisle, Casey Stannard, Megan Windsor Reid, Pamela J. Pilgrim, David B. |
author_facet | Prill, Kendal Carlisle, Casey Stannard, Megan Windsor Reid, Pamela J. Pilgrim, David B. |
author_sort | Prill, Kendal |
collection | PubMed |
description | The structure and function of the sarcomere of striated muscle is well studied but the steps of sarcomere assembly and maintenance remain under-characterized. With the aid of chaperones and factors of the protein quality control system, muscle proteins can be folded and assembled into the contractile apparatus of the sarcomere. When sarcomere assembly is incomplete or the sarcomere becomes damaged, suites of chaperones and maintenance factors respond to repair the sarcomere. Here we show evidence of the importance of the M-line proteins, specifically myomesin, in the monitoring of sarcomere assembly and integrity in previously characterized zebrafish muscle mutants. We show that myomesin is one of the last proteins to be incorporated into the assembling sarcomere, and that in skeletal muscle, its incorporation requires connections with both titin and myosin. In diseased zebrafish sarcomeres, myomesin1a shows an early increase of gene expression, hours before chaperones respond to damaged muscle. We found that myomesin expression is also more specific to sarcomere damage than muscle creatine kinase, and our results and others support the use of myomesin assays as an early, specific, method of detecting muscle damage. |
format | Online Article Text |
id | pubmed-6808450 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-68084502019-11-02 Myomesin is part of an integrity pathway that responds to sarcomere damage and disease Prill, Kendal Carlisle, Casey Stannard, Megan Windsor Reid, Pamela J. Pilgrim, David B. PLoS One Research Article The structure and function of the sarcomere of striated muscle is well studied but the steps of sarcomere assembly and maintenance remain under-characterized. With the aid of chaperones and factors of the protein quality control system, muscle proteins can be folded and assembled into the contractile apparatus of the sarcomere. When sarcomere assembly is incomplete or the sarcomere becomes damaged, suites of chaperones and maintenance factors respond to repair the sarcomere. Here we show evidence of the importance of the M-line proteins, specifically myomesin, in the monitoring of sarcomere assembly and integrity in previously characterized zebrafish muscle mutants. We show that myomesin is one of the last proteins to be incorporated into the assembling sarcomere, and that in skeletal muscle, its incorporation requires connections with both titin and myosin. In diseased zebrafish sarcomeres, myomesin1a shows an early increase of gene expression, hours before chaperones respond to damaged muscle. We found that myomesin expression is also more specific to sarcomere damage than muscle creatine kinase, and our results and others support the use of myomesin assays as an early, specific, method of detecting muscle damage. Public Library of Science 2019-10-23 /pmc/articles/PMC6808450/ /pubmed/31644553 http://dx.doi.org/10.1371/journal.pone.0224206 Text en © 2019 Prill et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | Research Article Prill, Kendal Carlisle, Casey Stannard, Megan Windsor Reid, Pamela J. Pilgrim, David B. Myomesin is part of an integrity pathway that responds to sarcomere damage and disease |
title | Myomesin is part of an integrity pathway that responds to sarcomere damage and disease |
title_full | Myomesin is part of an integrity pathway that responds to sarcomere damage and disease |
title_fullStr | Myomesin is part of an integrity pathway that responds to sarcomere damage and disease |
title_full_unstemmed | Myomesin is part of an integrity pathway that responds to sarcomere damage and disease |
title_short | Myomesin is part of an integrity pathway that responds to sarcomere damage and disease |
title_sort | myomesin is part of an integrity pathway that responds to sarcomere damage and disease |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6808450/ https://www.ncbi.nlm.nih.gov/pubmed/31644553 http://dx.doi.org/10.1371/journal.pone.0224206 |
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