Dystrophy-associated caveolin-3 mutations reveal that caveolae couple IL6/STAT3 signaling with mechanosensing in human muscle cells

Caveolae are mechanosensors and mutations of their coat proteins are implicated in muscle disorders, but molecular mechanisms are unclear. Here, the authors show that caveolae can regulate IL6/STAT3 signaling in muscle cells under stress, and that dystrophy related Cav3 mutant myotubes have reduced...

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Main Authors: Melissa Dewulf, Darius Vasco Köster, Bidisha Sinha, Christine Viaris de Lesegno, Valérie Chambon, Anne Bigot, Mona Bensalah, Elisa Negroni, Nicolas Tardif, Joanna Podkalicka, Ludger Johannes, Pierre Nassoy, Gillian Butler-Browne, Christophe Lamaze, Cedric M. Blouin
Format: Article
Language:English
Published: Nature Publishing Group 2019-04-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-019-09405-5
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spelling doaj-af0a410ef64d4e98b3b78ef974859a6d2021-05-11T11:53:26ZengNature Publishing GroupNature Communications2041-17232019-04-0110111310.1038/s41467-019-09405-5Dystrophy-associated caveolin-3 mutations reveal that caveolae couple IL6/STAT3 signaling with mechanosensing in human muscle cellsMelissa Dewulf0Darius Vasco Köster1Bidisha Sinha2Christine Viaris de Lesegno3Valérie Chambon4Anne Bigot5Mona Bensalah6Elisa Negroni7Nicolas Tardif8Joanna Podkalicka9Ludger Johannes10Pierre Nassoy11Gillian Butler-Browne12Christophe Lamaze13Cedric M. Blouin14Membrane Dynamics and Mechanics of Intracellular Signaling Laboratory, Institut Curie – Centre de Recherche, PSL Research University, CNRS UMR3666, INSERM U1143Centre for Mechanochemical Cell Biology and Division of Biomedical Sciences, Warwick Medical School, University of WarwickDepartment of Biological Sciences, Indian Institute of Science Education and Research (IISER) KolkataMembrane Dynamics and Mechanics of Intracellular Signaling Laboratory, Institut Curie – Centre de Recherche, PSL Research University, CNRS UMR3666, INSERM U1143Endocytic Trafficking and Intracellular Delivery Laboratory, Institut Curie – Centre de Recherche, PSL Research University, CNRS UMR3666, INSERM U1143Association Institut de Myologie, Centre de Recherche en Myologie, Sorbonne Université, INSERM, UMRS974Association Institut de Myologie, Centre de Recherche en Myologie, Sorbonne Université, INSERM, UMRS974Association Institut de Myologie, Centre de Recherche en Myologie, Sorbonne Université, INSERM, UMRS974Membrane Dynamics and Mechanics of Intracellular Signaling Laboratory, Institut Curie – Centre de Recherche, PSL Research University, CNRS UMR3666, INSERM U1143Membrane Dynamics and Mechanics of Intracellular Signaling Laboratory, Institut Curie – Centre de Recherche, PSL Research University, CNRS UMR3666, INSERM U1143Endocytic Trafficking and Intracellular Delivery Laboratory, Institut Curie – Centre de Recherche, PSL Research University, CNRS UMR3666, INSERM U1143LP2N, CNRS UMR 5298, IOA, Institut d’Optique Graduate School, Université de BordeauxAssociation Institut de Myologie, Centre de Recherche en Myologie, Sorbonne Université, INSERM, UMRS974Membrane Dynamics and Mechanics of Intracellular Signaling Laboratory, Institut Curie – Centre de Recherche, PSL Research University, CNRS UMR3666, INSERM U1143Membrane Dynamics and Mechanics of Intracellular Signaling Laboratory, Institut Curie – Centre de Recherche, PSL Research University, CNRS UMR3666, INSERM U1143Caveolae are mechanosensors and mutations of their coat proteins are implicated in muscle disorders, but molecular mechanisms are unclear. Here, the authors show that caveolae can regulate IL6/STAT3 signaling in muscle cells under stress, and that dystrophy related Cav3 mutant myotubes have reduced caveolae and upregulated IL6 signaling.https://doi.org/10.1038/s41467-019-09405-5
collection DOAJ
language English
format Article
sources DOAJ
author Melissa Dewulf
Darius Vasco Köster
Bidisha Sinha
Christine Viaris de Lesegno
Valérie Chambon
Anne Bigot
Mona Bensalah
Elisa Negroni
Nicolas Tardif
Joanna Podkalicka
Ludger Johannes
Pierre Nassoy
Gillian Butler-Browne
Christophe Lamaze
Cedric M. Blouin
spellingShingle Melissa Dewulf
Darius Vasco Köster
Bidisha Sinha
Christine Viaris de Lesegno
Valérie Chambon
Anne Bigot
Mona Bensalah
Elisa Negroni
Nicolas Tardif
Joanna Podkalicka
Ludger Johannes
Pierre Nassoy
Gillian Butler-Browne
Christophe Lamaze
Cedric M. Blouin
Dystrophy-associated caveolin-3 mutations reveal that caveolae couple IL6/STAT3 signaling with mechanosensing in human muscle cells
Nature Communications
author_facet Melissa Dewulf
Darius Vasco Köster
Bidisha Sinha
Christine Viaris de Lesegno
Valérie Chambon
Anne Bigot
Mona Bensalah
Elisa Negroni
Nicolas Tardif
Joanna Podkalicka
Ludger Johannes
Pierre Nassoy
Gillian Butler-Browne
Christophe Lamaze
Cedric M. Blouin
author_sort Melissa Dewulf
title Dystrophy-associated caveolin-3 mutations reveal that caveolae couple IL6/STAT3 signaling with mechanosensing in human muscle cells
title_short Dystrophy-associated caveolin-3 mutations reveal that caveolae couple IL6/STAT3 signaling with mechanosensing in human muscle cells
title_full Dystrophy-associated caveolin-3 mutations reveal that caveolae couple IL6/STAT3 signaling with mechanosensing in human muscle cells
title_fullStr Dystrophy-associated caveolin-3 mutations reveal that caveolae couple IL6/STAT3 signaling with mechanosensing in human muscle cells
title_full_unstemmed Dystrophy-associated caveolin-3 mutations reveal that caveolae couple IL6/STAT3 signaling with mechanosensing in human muscle cells
title_sort dystrophy-associated caveolin-3 mutations reveal that caveolae couple il6/stat3 signaling with mechanosensing in human muscle cells
publisher Nature Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2019-04-01
description Caveolae are mechanosensors and mutations of their coat proteins are implicated in muscle disorders, but molecular mechanisms are unclear. Here, the authors show that caveolae can regulate IL6/STAT3 signaling in muscle cells under stress, and that dystrophy related Cav3 mutant myotubes have reduced caveolae and upregulated IL6 signaling.
url https://doi.org/10.1038/s41467-019-09405-5
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