3D mapping of the SPRY2 domain of ryanodine receptor 1 by single-particle cryo-EM

Perálvarez-Marin, A, Tae, H, Board, P, Casarotto, M, Dulhunty, A and Samsó, M 2011, '3D mapping of the SPRY2 domain of ryanodine receptor 1 by single-particle cryo-EM', PLoS ONE, vol. 6, no. 10, e25813, pp. 1-7.

Document type: Journal Article
Collection: Journal Articles

Title 3D mapping of the SPRY2 domain of ryanodine receptor 1 by single-particle cryo-EM
Author(s) Perálvarez-Marin, A
Tae, H
Board, P
Casarotto, M
Dulhunty, A
Samsó, M
Year 2011
Journal name PLoS ONE
Volume number 6
Issue number 10
Article Number e25813
Start page 1
End page 7
Total pages 7
Publisher Public Library of Science
Abstract The type 1 skeletal muscle ryanodine receptor (RyR1) is principally responsible for Ca2+ release from the sarcoplasmic reticulum and for the subsequent muscle contraction. The RyR1 contains three SPRY domains. SPRY domains are generally known to mediate protein-protein interactions, however the location of the three SPRY domains in the 3D structure of the RyR1 is not known. Combining immunolabeling and single-particle cryo-electron microscopy we have mapped the SPRY2 domain (S1085-V1208) in the 3D structure of RyR1 using three different antibodies against the SPRY2 domain. Two obstacles for the image processing procedure; limited amount of data and signal dilution introduced by the multiple orientations of the antibody bound in the tetrameric RyR1, were overcome by modifying the 3D reconstruction scheme. This approach enabled us to ascertain that the three antibodies bind to the same region, to obtain a 3D reconstruction of RyR1 with the antibody bound, and to map SPRY2 to the periphery of the cytoplasmic domain of RyR1. We report here the first 3D localization of a SPRY2 domain in any known RyR isoform.
Subject Medical Physiology not elsewhere classified
DOI - identifier 10.1371/journal.pone.0025813
Copyright notice © 2011 Peralvarez-Maryn et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
ISSN 1932-6203
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Citation counts: TR Web of Science Citation Count  Cited 13 times in Thomson Reuters Web of Science Article | Citations
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