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Cited by 67Advanced Electron Microscopy Techniques and ApplicationsCardiomyopathy and Myosin StudiesProtein Structure and Dynamics

Molecular-scale visualization of sarcomere contraction within native cardiomyocytes

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Burbaum, Laura, Schneider, Jonathan, Scholze, Sarah, Böttcher, Ralph T., Baumeister, Wolfgang, Schwille, Petra, Plitzko, Jürgen M., Jasnin, Marion·2021·Nature Communications
DOI 10.1038/s41467-021-24049-0PMC PMC8253822

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Abstract

Sarcomeres, the basic contractile units of striated muscle, produce the forces driving muscular contraction through cross-bridge interactions between actin-containing thin filaments and myosin II-based thick filaments. Until now, direct visualization of the molecular architecture underlying sarcomere contractility has remained elusive. Here, we use in situ cryo-electron tomography to unveil sarcomere contraction in frozen-hydrated neonatal rat cardiomyocytes. We show that the hexagonal lattice of the thick filaments is already established at the neonatal stage, with an excess of thin filaments outside the trigonal positions. Structural assessment of actin polarity by subtomogram averaging reveals that thin filaments in the fully activated state form overlapping arrays of opposite polarity in the center of the sarcomere. Our approach provides direct evidence for thin filament sliding during muscle contraction and may serve as a basis for structural understanding of thin filament activation and actomyosin interactions inside unperturbed cellular environments.

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  • The Z-line and M-line are where myofilaments are entangled with particularly higher density.

    “The Z-line and M-line are where the myofilaments are entangled of particularly higher density (Fig. 3A) (30).”

    From Light diffraction by sarcomeres produces iridescence in transmission in the transparent ghost catfish (2023) · cites this paper as [30]

    In ‘Visualizing the myofibrillar interior in situ’ (page unavailable), the paper describes Z-disks as densely packed structures with high density. In ‘Structural signature of sarcomere contraction’ (page unavailable), it reports filament overlap at two of three M-lines, but says it did not observe a significant increase in thin-filament number in those regions. The claim’s higher-density characterization of the M-line is therefore not supported. (LLM, conf=0.87)

    Experimental — accuracy not yet measured

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Authors
Burbaum, L., Schneider, J., Scholze, S., Böttcher, R. T., Baumeister, W., Schwille, P., Plitzko, J. M., & Jasnin, M.
Affiliations
Max Planck Institute of Biochemistry (DE)
Corresponding author
Jasnin, Marion
ORCID
Venue
Nature Communications
Publisher
Springer Science and Business Media LLC
Published
2021-07-02
Volume
12
Issue
1
Pages
4086-4086
ISSN
2041-1723 (ISSN-L)
DOI
10.1038/s41467-021-24049-0
PMC
PMC8253822
OpenAlex
W3173393387
Cited by
67
References
1
Citations by year
2026: 8 · 2025: 14 · 2024: 12 · 2023: 9 · 2022: 13 · 2021: 10 · 2020: 1
FWCI
4.74
Type
journal article
Language
en
Open access
Licence
Locations
  • Nature Communications (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • RePEc: Research Papers in Economics (submittedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
  • Deutsches Zentrum für Herz-Kreislaufforschung
  • Max-Planck-Gesellschaft
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Advanced Electron Microscopy Techniques and Applications
  • Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiomyopathy and Myosin Studies
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Keywords
sarcomere contraction, cardiomyocytes, actin polarity, actomyosin, thin filament activation, neonatal rat heart, cryo-electron tomography, subtomogram averaging
MeSH terms
Actins, Animals, Male, Mice, Inbred C57BL, Actin Cytoskeleton, Muscle Contraction, Myofibrils, Sarcomeres, Rats, Wistar, Muscle, Skeletal, Myocytes, Cardiac, Mice, Rats, Muscle, Striated

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