Structure of RyR1 in native membranes.

EMBO Reports
Wenbo Chen, Mikhail Kudryashev

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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Citations

Jul 19, 2020·Proceedings of the National Academy of Sciences of the United States of America·Xia YaoNieng Yan
Nov 10, 2020·Canadian Journal of Physiology and Pharmacology·C PalahniukJ S C Gilchrist
Dec 24, 2020·Trends in Biochemical Sciences·Deshun GongHannah A Ledford
Jul 20, 2021·Physiological Reviews·Kellie A Woll, Filip Van Petegem

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Methods Mentioned

BETA
electron microscopy
PCA

Software Mentioned

TMHMM
SerialEM
dynamo
Relion
IMOD
analyze
fsc
MotionCor2
ccmartix

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