Cargando…

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,...

Descripción completa

Detalles Bibliográficos
Autores principales: Gutiérrez-Pérez, Paula, Santillán, Emilio M., Lendl, Thomas, Wang, Jingkui, Schrempf, Anna, Steinacker, Thomas L., Asparuhova, Mila, Brandstetter, Marlene, Haselbach, David, Cochella, Luisa
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Association for the Advancement of Science 2021
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
_version_ 1784584480944553984
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
work_keys_str_mv AT gutierrezperezpaula mir1sustainsmusclephysiologybycontrollingvatpasecomplexassembly
AT santillanemiliom mir1sustainsmusclephysiologybycontrollingvatpasecomplexassembly
AT lendlthomas mir1sustainsmusclephysiologybycontrollingvatpasecomplexassembly
AT wangjingkui mir1sustainsmusclephysiologybycontrollingvatpasecomplexassembly
AT schrempfanna mir1sustainsmusclephysiologybycontrollingvatpasecomplexassembly
AT steinackerthomasl mir1sustainsmusclephysiologybycontrollingvatpasecomplexassembly
AT asparuhovamila mir1sustainsmusclephysiologybycontrollingvatpasecomplexassembly
AT brandstettermarlene mir1sustainsmusclephysiologybycontrollingvatpasecomplexassembly
AT haselbachdavid mir1sustainsmusclephysiologybycontrollingvatpasecomplexassembly
AT cochellaluisa mir1sustainsmusclephysiologybycontrollingvatpasecomplexassembly