Arginylation of myosin heavy chain regulates skeletal muscle strength
Copyright © 2014 The Authors. Published by Elsevier Inc. All rights reserved..
Protein arginylation is a posttranslational modification with an emerging global role in the regulation of actin cytoskeleton. To test the role of arginylation in the skeletal muscle, we generated a mouse model with Ate1 deletion driven by the skeletal muscle-specific creatine kinase (Ckmm) promoter. Ckmm-Ate1 mice were viable and outwardly normal; however, their skeletal muscle strength was significantly reduced in comparison to controls. Mass spectrometry of isolated skeletal myofibrils showed a limited set of proteins, including myosin heavy chain, arginylated on specific sites. Atomic force microscopy measurements of contractile strength in individual myofibrils and isolated myosin filaments from these mice showed a significant reduction of contractile forces, which, in the case of myosin filaments, could be fully rescued by rearginylation with purified Ate1. Our results demonstrate that arginylation regulates force production in muscle and exerts a direct effect on muscle strength through arginylation of myosin.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2014 |
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| Erschienen: |
2014 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:8 |
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| Enthalten in: |
Cell reports - 8(2014), 2 vom: 24. Juli, Seite 470-6 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Cornachione, Anabelle S [VerfasserIn] |
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| Links: |
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| Themen: |
Aminoacyltransferases |
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| Anmerkungen: |
Date Completed 21.08.2015 Date Revised 21.10.2021 published: Print-Electronic Citation Status MEDLINE |
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| doi: |
10.1016/j.celrep.2014.06.019 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| 245 | 1 | 0 | |a Arginylation of myosin heavy chain regulates skeletal muscle strength |
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| 520 | |a Copyright © 2014 The Authors. Published by Elsevier Inc. All rights reserved. | ||
| 520 | |a Protein arginylation is a posttranslational modification with an emerging global role in the regulation of actin cytoskeleton. To test the role of arginylation in the skeletal muscle, we generated a mouse model with Ate1 deletion driven by the skeletal muscle-specific creatine kinase (Ckmm) promoter. Ckmm-Ate1 mice were viable and outwardly normal; however, their skeletal muscle strength was significantly reduced in comparison to controls. Mass spectrometry of isolated skeletal myofibrils showed a limited set of proteins, including myosin heavy chain, arginylated on specific sites. Atomic force microscopy measurements of contractile strength in individual myofibrils and isolated myosin filaments from these mice showed a significant reduction of contractile forces, which, in the case of myosin filaments, could be fully rescued by rearginylation with purified Ate1. Our results demonstrate that arginylation regulates force production in muscle and exerts a direct effect on muscle strength through arginylation of myosin | ||
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| 700 | 1 | |a Wang, Junling |e verfasserin |4 aut | |
| 700 | 1 | |a Leu, Nicolae A |e verfasserin |4 aut | |
| 700 | 1 | |a Kalganov, Albert |e verfasserin |4 aut | |
| 700 | 1 | |a Volgin, Denys |e verfasserin |4 aut | |
| 700 | 1 | |a Han, Xuemei |e verfasserin |4 aut | |
| 700 | 1 | |a Xu, Tao |e verfasserin |4 aut | |
| 700 | 1 | |a Cheng, Yu-Shu |e verfasserin |4 aut | |
| 700 | 1 | |a Yates, John R R |c 3rd |e verfasserin |4 aut | |
| 700 | 1 | |a Rassier, Dilson E |e verfasserin |4 aut | |
| 700 | 1 | |a Kashina, Anna |e verfasserin |4 aut | |
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