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  Molecular-scale visualization of sarcomere contraction within native cardiomyocytes

Burbaum, L., Schneider, J., Scholze, S., Böttcher, R. T., Baumeister, W., Schwille, P., et al. (2021). Molecular-scale visualization of sarcomere contraction within native cardiomyocytes. Nature Communications, 12(1): 4086. doi:10.1038/s41467-021-24049-0.

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 Creators:
Burbaum, Laura1, Author           
Schneider, Jonathan2, Author           
Scholze, Sarah3, Author           
Böttcher, Ralph T.3, Author           
Baumeister, Wolfgang2, Author           
Schwille, Petra1, Author           
Plitzko, Jürgen M.2, Author           
Jasnin, Marion2, Author           
Affiliations:
1Schwille, Petra / Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565169              
2Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              
3Fässler, Reinhard / Molecular Medicine, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565147              

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Free keywords: X-RAY-DIFFRACTION; CRYOELECTRON TOMOGRAPHY; ELECTRON-MICROSCOPE; STRIATED-MUSCLE; CARDIAC-MUSCLE; FILAMENT; LATTICE; ACTIN; CELL; ARCHITECTUREScience & Technology - Other Topics;
 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. Sarcomeres, the building blocks of striated muscles, comprise ordered actomyosin arrays involved in force production. Here, the authors visualize sarcomere organization in neonatal cardiomyocytes with in situ cryo-electron tomography, revealing a reduced order of the thin filaments, their sliding and functional states enabling contraction.

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Language(s): eng - English
 Dates: 2021
 Publication Status: Published online
 Pages: 12
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

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Title: Nature Communications
  Abbreviation : Nat. Commun.
Source Genre: Journal
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Publ. Info: London : Nature Publishing Group
Pages: - Volume / Issue: 12 (1) Sequence Number: 4086 Start / End Page: - Identifier: ISSN: 2041-1723
CoNE: https://pure.mpg.de/cone/journals/resource/2041-1723