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miR-1 sustains muscle physiology by controlling V-ATPase complex assembly
Muscle function requires unique structural and metabolic adaptations that can render muscle cells selectively vulnerable, with mutations in some ubiquitously expressed genes causing myopathies but sparing other tissues. We uncovered a muscle cell vulnerability by studying miR-1, a deeply conserved,...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Association for the Advancement of Science
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8519577/ https://www.ncbi.nlm.nih.gov/pubmed/34652942 http://dx.doi.org/10.1126/sciadv.abh1434 |
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author | Gutiérrez-Pérez, Paula Santillán, Emilio M. Lendl, Thomas Wang, Jingkui Schrempf, Anna Steinacker, Thomas L. Asparuhova, Mila Brandstetter, Marlene Haselbach, David Cochella, Luisa |
author_facet | Gutiérrez-Pérez, Paula Santillán, Emilio M. Lendl, Thomas Wang, Jingkui Schrempf, Anna Steinacker, Thomas L. Asparuhova, Mila Brandstetter, Marlene Haselbach, David Cochella, Luisa |
author_sort | Gutiérrez-Pérez, Paula |
collection | PubMed |
description | Muscle function requires unique structural and metabolic adaptations that can render muscle cells selectively vulnerable, with mutations in some ubiquitously expressed genes causing myopathies but sparing other tissues. We uncovered a muscle cell vulnerability by studying miR-1, a deeply conserved, muscle-specific microRNA whose ablation causes various muscle defects. Using Caenorhabditis elegans, we found that miR-1 represses multiple subunits of the ubiquitous vacuolar adenosine triphosphatase (V-ATPase) complex, which is essential for internal compartment acidification and metabolic signaling. V-ATPase subunits are predicted miR-1 targets in animals ranging from C. elegans to humans, and we experimentally validated this in Drosophila. Unexpectedly, up-regulation of V-ATPase subunits upon miR-1 deletion causes reduced V-ATPase function due to defects in complex assembly. These results reveal V-ATPase assembly as a conserved muscle cell vulnerability and support a previously unknown role for microRNAs in the regulation of protein complexes. |
format | Online Article Text |
id | pubmed-8519577 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | American Association for the Advancement of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-85195772021-10-26 miR-1 sustains muscle physiology by controlling V-ATPase complex assembly Gutiérrez-Pérez, Paula Santillán, Emilio M. Lendl, Thomas Wang, Jingkui Schrempf, Anna Steinacker, Thomas L. Asparuhova, Mila Brandstetter, Marlene Haselbach, David Cochella, Luisa Sci Adv Biomedicine and Life Sciences Muscle function requires unique structural and metabolic adaptations that can render muscle cells selectively vulnerable, with mutations in some ubiquitously expressed genes causing myopathies but sparing other tissues. We uncovered a muscle cell vulnerability by studying miR-1, a deeply conserved, muscle-specific microRNA whose ablation causes various muscle defects. Using Caenorhabditis elegans, we found that miR-1 represses multiple subunits of the ubiquitous vacuolar adenosine triphosphatase (V-ATPase) complex, which is essential for internal compartment acidification and metabolic signaling. V-ATPase subunits are predicted miR-1 targets in animals ranging from C. elegans to humans, and we experimentally validated this in Drosophila. Unexpectedly, up-regulation of V-ATPase subunits upon miR-1 deletion causes reduced V-ATPase function due to defects in complex assembly. These results reveal V-ATPase assembly as a conserved muscle cell vulnerability and support a previously unknown role for microRNAs in the regulation of protein complexes. American Association for the Advancement of Science 2021-10-15 /pmc/articles/PMC8519577/ /pubmed/34652942 http://dx.doi.org/10.1126/sciadv.abh1434 Text en Copyright © 2021 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution License 4.0 (CC BY). https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution license (https://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Biomedicine and Life Sciences Gutiérrez-Pérez, Paula Santillán, Emilio M. Lendl, Thomas Wang, Jingkui Schrempf, Anna Steinacker, Thomas L. Asparuhova, Mila Brandstetter, Marlene Haselbach, David Cochella, Luisa miR-1 sustains muscle physiology by controlling V-ATPase complex assembly |
title | miR-1 sustains muscle physiology by controlling V-ATPase complex assembly |
title_full | miR-1 sustains muscle physiology by controlling V-ATPase complex assembly |
title_fullStr | miR-1 sustains muscle physiology by controlling V-ATPase complex assembly |
title_full_unstemmed | miR-1 sustains muscle physiology by controlling V-ATPase complex assembly |
title_short | miR-1 sustains muscle physiology by controlling V-ATPase complex assembly |
title_sort | mir-1 sustains muscle physiology by controlling v-atpase complex assembly |
topic | Biomedicine and Life Sciences |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8519577/ https://www.ncbi.nlm.nih.gov/pubmed/34652942 http://dx.doi.org/10.1126/sciadv.abh1434 |
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