Molecular-scale visualization of sarcomere contraction within native cardiomyocytes

Laura Burbaum, Jonathan Schneider, Sarah Scholze, Ralph T. Böttcher, Wolfgang Baumeister, Petra Schwille, Jürgen M. Plitzko and Marion Jasnin ()
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Laura Burbaum: Max Planck Institute of Biochemistry
Jonathan Schneider: Max Planck Institute of Biochemistry
Sarah Scholze: Max Planck Institute of Biochemistry
Ralph T. Böttcher: Max Planck Institute of Biochemistry
Wolfgang Baumeister: Max Planck Institute of Biochemistry
Petra Schwille: Max Planck Institute of Biochemistry
Jürgen M. Plitzko: Max Planck Institute of Biochemistry
Marion Jasnin: Max Planck Institute of Biochemistry

Nature Communications, 2021, vol. 12, issue 1, 1-12

Abstract: 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.

Date: 2021
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-24049-0

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DOI: 10.1038/s41467-021-24049-0

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