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  Polarization-resolved microscopy reveals a muscle myosin motor-independent mechanism of molecular actin ordering during sarcomere maturation

Loison, O., Weitkunat, M., Kaya-Copur, A., Alves, C. N., Matzat, T., Spletter, M. L., et al. (2018). Polarization-resolved microscopy reveals a muscle myosin motor-independent mechanism of molecular actin ordering during sarcomere maturation. PLoS Biology, 16(4): e2004718. doi:10.1371/journal.pbio.2004718.

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 Creators:
Loison, Olivier1, Author
Weitkunat, Manuela2, Author              
Kaya-Copur, Aynur2, Author              
Alves, Camila Nascimento1, Author
Matzat, Till1, Author
Spletter, Maria L.2, Author              
Luschnig, Stefan1, Author
Brasselet, Sophie1, Author
Lenne, Pierre-Francois1, Author
Schnorrer, Frank2, Author              
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1external, ou_persistent22              
2Schnorrer, Frank / Muscle Dynamics, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565168              

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Free keywords: DROSOPHILA FLIGHT-MUSCLE; IN-VIVO; TRANSGENIC RNAI; THICK FILAMENTS; MYOFIBRILLOGENESIS; MYOFIBRILS; DYNAMICS; HEART; SPEED; ORGANIZATIONBiochemistry & Molecular Biology; Life Sciences & Biomedicine - Other Topics;
 Abstract: Sarcomeres are stereotyped force-producing mini-machines of striated muscles. Each sarcomere contains a pseudocrystalline order of bipolar actin and myosin filaments, which are linked by titin filaments. During muscle development, these three filament types need to assemble into long periodic chains of sarcomeres called myofibrils. Initially, myofibrils contain immature sarcomeres, which gradually mature into their pseudocrystalline order. Despite the general importance, our understanding of myofibril assembly and sarcomere maturation in vivo is limited, in large part because determining the molecular order of protein components during muscle development remains challenging. Here, we applied polarization-resolved microscopy to determine the molecular order of actin during myofibrillogenesis in vivo. This method revealed that, concomitantly with mechanical tension buildup in the myotube, molecular actin order increases, preceding the formation of immature sarcomeres. Mechanistically, both muscle and nonmuscle myosin contribute to this actin order gain during early stages of myofibril assembly. Actin order continues to increase while myofibrils and sarcomeres mature. Muscle myosin motor activity is required for the regular and coordinated assembly of long myofibrils but not for the high actin order buildup during sarcomere maturation. This suggests that, in muscle, other actin-binding proteins are sufficient to locally bundle or cross-link actin into highly regular arrays.

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Language(s): eng - English
 Dates: 2018
 Publication Status: Published online
 Pages: 25
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Title: PLoS Biology
  Other : PLoS Biol.
Source Genre: Journal
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Publ. Info: San Francisco, California, US : Public Library of Science
Pages: - Volume / Issue: 16 (4) Sequence Number: e2004718 Start / End Page: - Identifier: ISSN: 1544-9173
CoNE: https://pure.mpg.de/cone/journals/resource/111056649444170