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Structure of RyR1 in native membranes

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Item Type:Article
Title:Structure of RyR1 in native membranes
Creators Name:Chen, W. and Kudryashev, M.
Abstract:Ryanodine receptor 1 (RyR1) mediates excitation-contraction coupling by releasing Ca(2+) 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.
Keywords:Cryo-Electron Tomography, Muscle Contraction, Ryanodine Receptor, Sarcoplasmic Reticulum, Subtomogram Averaging, Animals, Rabbits
Source:EMBO Reports
ISSN:1469-221X
Publisher:Nature Publishing Group
Volume:21
Number:5
Page Range:e49891
Date:6 May 2020
Official Publication:https://doi.org/10.15252/embr.201949891
PubMed:View item in PubMed

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