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  Structure of RyR1 in native membranes

Chen, W., & Kudryashev, M. (2020). Structure of RyR1 in native membranes. EMBO Reports, 21(5): e49891. doi:10.15252/embr.201949891.

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Genre: Journal Article

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 Creators:
Chen, Wenbo1, 2, Author              
Kudryashev, Mikhail1, 2, Author              
Affiliations:
1Sofja Kovalevskaja Group, Max Planck Institute of Biophysics, Max Planck Society, ou_2253651              
2Buchmann Institute for Molecular Life Sciences, Goethe University Frankfurt, Frankfurt on Main, Germany, ou_persistent22              

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Free keywords: cryo-electron tomography, muscle contraction, ryanodine receptor, sarcoplasmic reticulum, subtomogram averaging
 Abstract: Ryanodine receptor 1 (RyR1) mediates excitation-contraction coupling by releasing Ca2+ from sarcoplasmic reticulum (SR) to the cytoplasm of skeletal muscle cells. RyR1 activation is regulated by several proteins from both the cytoplasm and lumen of the SR. Here, we report the structure of RyR1 from native SR membranes in closed and open states. Compared to the previously reported structures of purified RyR1, our structure reveals helix-like densities traversing the bilayer approximately 5 nm from the RyR1 transmembrane domain and sarcoplasmic extensions linking RyR1 to a putative calsequestrin network. We document the primary conformation of RyR1 in situ and its structural variations. The activation of RyR1 is associated with changes in membrane curvature and movement in the sarcoplasmic extensions. Our results provide structural insight into the mechanism of RyR1 in its native environment.

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Language(s): eng - English
 Dates: 2020-02-102019-12-132020-02-142020-03-09
 Publication Status: Published online
 Pages: 11
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.15252/embr.201949891
BibTex Citekey: chen_structure_2020
 Degree: -

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Title: EMBO Reports
  Other : EMBO Rep.
Source Genre: Journal
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Publ. Info: Oxford, UK : Published for EMBO by Oxford University Press
Pages: - Volume / Issue: 21 (5) Sequence Number: e49891 Start / End Page: - Identifier: ISSN: 1469-221X
CoNE: https://pure.mpg.de/cone/journals/resource/110978984569661