ZAKβ is activated by cellular compression and mediates contraction‐induced MAP kinase signaling in skeletal muscle
Mechanical inputs give rise to p38 and JNK activation, which mediate adaptive physiological responses in various tissues. In skeletal muscle, contraction‐induced p38 and JNK signaling ensure adaptation to exercise, muscle repair, and hypertrophy. However, the mechanisms by which muscle fibers sense...
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| Published in | The EMBO journal Vol. 41; no. 17; pp. e111650 - n/a |
|---|---|
| Main Authors | , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
London
Nature Publishing Group UK
01.09.2022
Springer Nature B.V EMBO Press John Wiley and Sons Inc |
| Subjects | |
| Online Access | Get full text |
| ISSN | 0261-4189 1460-2075 1460-2075 |
| DOI | 10.15252/embj.2022111650 |
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| Abstract | Mechanical inputs give rise to p38 and JNK activation, which mediate adaptive physiological responses in various tissues. In skeletal muscle, contraction‐induced p38 and JNK signaling ensure adaptation to exercise, muscle repair, and hypertrophy. However, the mechanisms by which muscle fibers sense mechanical load to activate this signaling have remained elusive. Here, we show that the upstream MAP3K ZAKβ is activated by cellular compression induced by osmotic shock and cyclic compression
in vitro
, and muscle contraction
in vivo
. This function relies on ZAKβ's ability to recognize stress fibers in cells and Z‐discs in muscle fibers when mechanically perturbed. Consequently, ZAK‐deficient mice present with skeletal muscle defects characterized by fibers with centralized nuclei and progressive adaptation towards a slower myosin profile. Our results highlight how cells in general respond to mechanical compressive load and how mechanical forces generated during muscle contraction are translated into MAP kinase signaling.
Synopsis
Mutations in the MAP3 kinase ZAKβ are associated with progressive muscle weakness in human patients. Here, ZAKβ is shown to protect against myopathy by inducing p38 and JNK signaling in response to mechanical stimuli.
ZAKβ is activated by hyperosmotic shock and compressive mechanical stimuli.
Mechanical stress‐dependent ZAKβ activation depends on its recruitment to stress fibers in human cell lines and Z‐discs in the skeletal muscle
Mice deficient for the ZAK gene show defects in p38 and JNK activation upon skeletal muscle contraction.
ZAK knockout mice display muscle pathologies that are reminiscent of human patients mutated in the ZAK gene.
Graphical Abstract
ZAKβ protects against myopathy by inducing p38 and JNK signaling in response to mechanical stimuli. |
|---|---|
| AbstractList | Mechanical inputs give rise to p38 and JNK activation, which mediate adaptive physiological responses in various tissues. In skeletal muscle, contraction‐induced p38 and JNK signaling ensure adaptation to exercise, muscle repair, and hypertrophy. However, the mechanisms by which muscle fibers sense mechanical load to activate this signaling have remained elusive. Here, we show that the upstream MAP3K ZAKβ is activated by cellular compression induced by osmotic shock and cyclic compression
in vitro
, and muscle contraction
in vivo
. This function relies on ZAKβ's ability to recognize stress fibers in cells and Z‐discs in muscle fibers when mechanically perturbed. Consequently, ZAK‐deficient mice present with skeletal muscle defects characterized by fibers with centralized nuclei and progressive adaptation towards a slower myosin profile. Our results highlight how cells in general respond to mechanical compressive load and how mechanical forces generated during muscle contraction are translated into MAP kinase signaling.
image
Mutations in the MAP3 kinase ZAKβ are associated with progressive muscle weakness in human patients. Here, ZAKβ is shown to protect against myopathy by inducing p38 and JNK signaling in response to mechanical stimuli.
ZAKβ is activated by hyperosmotic shock and compressive mechanical stimuli.
Mechanical stress‐dependent ZAKβ activation depends on its recruitment to stress fibers in human cell lines and Z‐discs in the skeletal muscle
Mice deficient for the ZAK gene show defects in p38 and JNK activation upon skeletal muscle contraction.
ZAK knockout mice display muscle pathologies that are reminiscent of human patients mutated in the ZAK gene. Mechanical inputs give rise to p38 and JNK activation, which mediate adaptive physiological responses in various tissues. In skeletal muscle, contraction-induced p38 and JNK signaling ensure adaptation to exercise, muscle repair, and hypertrophy. However, the mechanisms by which muscle fibers sense mechanical load to activate this signaling have remained elusive. Here, we show that the upstream MAP3K ZAKβ is activated by cellular compression induced by osmotic shock and cyclic compression in vitro, and muscle contraction in vivo. This function relies on ZAKβ's ability to recognize stress fibers in cells and Z-discs in muscle fibers when mechanically perturbed. Consequently, ZAK-deficient mice present with skeletal muscle defects characterized by fibers with centralized nuclei and progressive adaptation towards a slower myosin profile. Our results highlight how cells in general respond to mechanical compressive load and how mechanical forces generated during muscle contraction are translated into MAP kinase signaling.Mechanical inputs give rise to p38 and JNK activation, which mediate adaptive physiological responses in various tissues. In skeletal muscle, contraction-induced p38 and JNK signaling ensure adaptation to exercise, muscle repair, and hypertrophy. However, the mechanisms by which muscle fibers sense mechanical load to activate this signaling have remained elusive. Here, we show that the upstream MAP3K ZAKβ is activated by cellular compression induced by osmotic shock and cyclic compression in vitro, and muscle contraction in vivo. This function relies on ZAKβ's ability to recognize stress fibers in cells and Z-discs in muscle fibers when mechanically perturbed. Consequently, ZAK-deficient mice present with skeletal muscle defects characterized by fibers with centralized nuclei and progressive adaptation towards a slower myosin profile. Our results highlight how cells in general respond to mechanical compressive load and how mechanical forces generated during muscle contraction are translated into MAP kinase signaling. Mechanical inputs give rise to p38 and JNK activation, which mediate adaptive physiological responses in various tissues. In skeletal muscle, contraction-induced p38 and JNK signaling ensure adaptation to exercise, muscle repair, and hypertrophy. However, the mechanisms by which muscle fibers sense mechanical load to activate this signaling have remained elusive. Here, we show that the upstream MAP3K ZAKb is activated by cellular compression induced by osmotic shock and cyclic compression in vitro, and muscle contraction in vivo. This function relies on ZAKb's ability to recognize stress fibers in cells and Z-discs in muscle fibers when mechanically perturbed. Consequently, ZAK-deficient mice present with skeletal muscle defects characterized by fibers with centralized nuclei and progressive adaptation towards a slower myosin profile. Our results highlight how cells in general respond to mechanical compressive load and how mechanical forces generated during muscle contraction are translated into MAP kinase signaling. Mechanical inputs give rise to p38 and JNK activation, which mediate adaptive physiological responses in various tissues. In skeletal muscle, contraction‐induced p38 and JNK signaling ensure adaptation to exercise, muscle repair, and hypertrophy. However, the mechanisms by which muscle fibers sense mechanical load to activate this signaling have remained elusive. Here, we show that the upstream MAP3K ZAKβ is activated by cellular compression induced by osmotic shock and cyclic compression in vitro , and muscle contraction in vivo . This function relies on ZAKβ's ability to recognize stress fibers in cells and Z‐discs in muscle fibers when mechanically perturbed. Consequently, ZAK‐deficient mice present with skeletal muscle defects characterized by fibers with centralized nuclei and progressive adaptation towards a slower myosin profile. Our results highlight how cells in general respond to mechanical compressive load and how mechanical forces generated during muscle contraction are translated into MAP kinase signaling. Synopsis Mutations in the MAP3 kinase ZAKβ are associated with progressive muscle weakness in human patients. Here, ZAKβ is shown to protect against myopathy by inducing p38 and JNK signaling in response to mechanical stimuli. ZAKβ is activated by hyperosmotic shock and compressive mechanical stimuli. Mechanical stress‐dependent ZAKβ activation depends on its recruitment to stress fibers in human cell lines and Z‐discs in the skeletal muscle Mice deficient for the ZAK gene show defects in p38 and JNK activation upon skeletal muscle contraction. ZAK knockout mice display muscle pathologies that are reminiscent of human patients mutated in the ZAK gene. Graphical Abstract ZAKβ protects against myopathy by inducing p38 and JNK signaling in response to mechanical stimuli. Mechanical inputs give rise to p38 and JNK activation, which mediate adaptive physiological responses in various tissues. In skeletal muscle, contraction‐induced p38 and JNK signaling ensure adaptation to exercise, muscle repair, and hypertrophy. However, the mechanisms by which muscle fibers sense mechanical load to activate this signaling have remained elusive. Here, we show that the upstream MAP3K ZAKβ is activated by cellular compression induced by osmotic shock and cyclic compression in vitro, and muscle contraction in vivo. This function relies on ZAKβ's ability to recognize stress fibers in cells and Z‐discs in muscle fibers when mechanically perturbed. Consequently, ZAK‐deficient mice present with skeletal muscle defects characterized by fibers with centralized nuclei and progressive adaptation towards a slower myosin profile. Our results highlight how cells in general respond to mechanical compressive load and how mechanical forces generated during muscle contraction are translated into MAP kinase signaling. Mechanical inputs give rise to p38 and JNK activation, which mediate adaptive physiological responses in various tissues. In skeletal muscle, contraction‐induced p38 and JNK signaling ensure adaptation to exercise, muscle repair, and hypertrophy. However, the mechanisms by which muscle fibers sense mechanical load to activate this signaling have remained elusive. Here, we show that the upstream MAP3K ZAKβ is activated by cellular compression induced by osmotic shock and cyclic compression in vitro , and muscle contraction in vivo . This function relies on ZAKβ's ability to recognize stress fibers in cells and Z‐discs in muscle fibers when mechanically perturbed. Consequently, ZAK‐deficient mice present with skeletal muscle defects characterized by fibers with centralized nuclei and progressive adaptation towards a slower myosin profile. Our results highlight how cells in general respond to mechanical compressive load and how mechanical forces generated during muscle contraction are translated into MAP kinase signaling. ZAKβ protects against myopathy by inducing p38 and JNK signaling in response to mechanical stimuli. Mechanical inputs give rise to p38 and JNK activation, which mediate adaptive physiological responses in various tissues. In skeletal muscle, contraction‐induced p38 and JNK signaling ensure adaptation to exercise, muscle repair, and hypertrophy. However, the mechanisms by which muscle fibers sense mechanical load to activate this signaling have remained elusive. Here, we show that the upstream MAP3K ZAKβ is activated by cellular compression induced by osmotic shock and cyclic compression in vitro, and muscle contraction in vivo. This function relies on ZAKβ's ability to recognize stress fibers in cells and Z‐discs in muscle fibers when mechanically perturbed. Consequently, ZAK‐deficient mice present with skeletal muscle defects characterized by fibers with centralized nuclei and progressive adaptation towards a slower myosin profile. Our results highlight how cells in general respond to mechanical compressive load and how mechanical forces generated during muscle contraction are translated into MAP kinase signaling. Synopsis Mutations in the MAP3 kinase ZAKβ are associated with progressive muscle weakness in human patients. Here, ZAKβ is shown to protect against myopathy by inducing p38 and JNK signaling in response to mechanical stimuli. ZAKβ is activated by hyperosmotic shock and compressive mechanical stimuli. Mechanical stress‐dependent ZAKβ activation depends on its recruitment to stress fibers in human cell lines and Z‐discs in the skeletal muscle Mice deficient for the ZAK gene show defects in p38 and JNK activation upon skeletal muscle contraction. ZAK knockout mice display muscle pathologies that are reminiscent of human patients mutated in the ZAK gene. ZAKβ protects against myopathy by inducing p38 and JNK signaling in response to mechanical stimuli. |
| Author | Kassem, Moustapha Jørgensen, Nicolas Oldenburg Snieckute, Goda Miroshnikova, Yekaterina A Haahr, Peter Pennisi, Cristian Pablo Tiedje, Christopher Mallein‐Gerin, Frederic Kjøbsted, Rasmus Olsen, Jesper Velgaard Clemmensen, Christoffer Mazouzi, Abdelghani Li, Xiang Falk, Sarah Antas, Pedro Blanco, Gonzalo Andersen, Jesper Løvind Blasius, Melanie Li, Vivian SW Wickström, Sara A Del Val, Ana Martinez Perrier‐Groult, Emeline Jafari, Abbas Stonadge, Amy Jakobsen, Jens Rithamer Nordgaard, Cathrine Vind, Anna Constance Reinert, Marie Sofie Brummelkamp, Thijn Wojtaszewski, Jørgen FP Bekker‐Jensen, Dorte Breinholdt Bekker‐Jensen, Simon |
| AuthorAffiliation | 13 Department of Endocrinology and Metabolism University Hospital of Odense and University of Southern Denmark Odense Denmark 15 CeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences Vienna Austria 3 Department of Nutrition, Exercise and Sports University of Copenhagen Copenhagen Denmark 5 Mass Spectrometry for Quantitative Proteomics, Proteomics Program, Faculty of Health and Medical Sciences, The Novo Nordisk Foundation Center for Protein Research University of Copenhagen Copenhagen Denmark 7 Stem Cells and Metabolism Research Program, Faculty of Medicine and Helsinki Institute of Life Science University of Helsinki Helsinki Finland 14 Oncode Institute, Division of Biochemistry The Netherlands Cancer Institute Amsterdam The Netherlands 12 Department of Cellular and Molecular Medicine, Novo Nordisk Foundation Center for Stem Cell Biology (DanStem) University of Copenhagen Copenhagen Denmark 4 Stem Cell and Cancer Biology Laboratory The Francis Crick Institute London |
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| Author_xml | – sequence: 1 givenname: Cathrine surname: Nordgaard fullname: Nordgaard, Cathrine organization: Center for Healthy Aging, Department of Cellular and Molecular Medicine, University of Copenhagen – sequence: 2 givenname: Anna Constance surname: Vind fullname: Vind, Anna Constance organization: Center for Healthy Aging, Department of Cellular and Molecular Medicine, University of Copenhagen – sequence: 3 givenname: Amy orcidid: 0000-0002-5381-0555 surname: Stonadge fullname: Stonadge, Amy organization: Department of Biology, University of York – sequence: 4 givenname: Rasmus surname: Kjøbsted fullname: Kjøbsted, Rasmus organization: Department of Nutrition, Exercise and Sports, University of Copenhagen – sequence: 5 givenname: Goda surname: Snieckute fullname: Snieckute, Goda organization: Center for Healthy Aging, Department of Cellular and Molecular Medicine, University of Copenhagen – sequence: 6 givenname: Pedro surname: Antas fullname: Antas, Pedro organization: Stem 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| Keywords | mechanobiology muscle contraction myopathy ZAKβ ZAKb Subject Categories Musculoskeletal System Post-translational Modifications & Proteolysis |
| Language | English |
| License | Attribution-NonCommercial-NoDerivs Distributed under a Creative Commons Attribution 4.0 International License: http://creativecommons.org/licenses/by/4.0 This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc-nd/4.0/ License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non‐commercial and no modifications or adaptations are made. |
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| SubjectTerms | Adaptation Cell lines Compression Compressive properties Defects EMBO25 EMBO31 Fibers Hypertrophy Kinases Life Sciences MAP kinase Mechanical properties Mechanical stimuli mechanobiology Muscle contraction Muscles Muscular function Musculoskeletal system Mutation Myopathy Myosin Osmotic shock Physiological responses Signaling Skeletal muscle Stimuli ZAKβ |
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| Title | ZAKβ is activated by cellular compression and mediates contraction‐induced MAP kinase signaling in skeletal muscle |
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