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Updated: Dec 26, 2025
07:59
Functional Characterization of Endogenously Expressed Human RYR1 Variants
Published on: June 9, 2021
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Structure of RyR1 in native membranes
Wenbo Chen1,2, Mikhail Kudryashev1,2
1Max Planck Institute for Biophysics, Frankfurt on Main, Germany.
EMBO Reports
|March 10, 2020
Summary
Ryanodine receptor 1 (RyR1) structures in skeletal muscle reveal its native conformation and activation mechanism. This study details RyR1
Area of Science:
- Muscle physiology
- Molecular biology
- Structural biology
Background:
- Ryanodine receptor 1 (RyR1) is crucial for skeletal muscle excitation-contraction coupling.
- RyR1 controls calcium (Ca2+) release from the sarcoplasmic reticulum (SR).
- RyR1 activity is modulated by associated proteins.
Purpose of the Study:
- To determine the structure of RyR1 in native SR membranes.
- To elucidate the structural changes associated with RyR1 activation.
- To understand RyR1's function in its native cellular environment.
Main Methods:
- Cryo-electron microscopy of RyR1 in native SR membranes.
- Structural analysis of RyR1 in closed and open states.
- In situ structural determination.
Main Results:
- Revealed novel helix-like densities near the RyR1 transmembrane domain.
- Identified sarcoplasmic extensions linking RyR1 to the calsequestrin network.
- Observed changes in membrane curvature and sarcoplasmic extensions upon RyR1 activation.
Conclusions:
- Provides the first in situ structural insights into RyR1 activation.
- Highlights the role of membrane interactions and sarcoplasmic extensions in RyR1 regulation.
- Enhances understanding of skeletal muscle excitation-contraction coupling.
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