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. 2017 Jul 24;7:6312. doi: 10.1038/s41598-017-06395-6

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© The Author(s) 2017

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Myospryn clusters RyR2 in heterologous cells. COS-7 cells were transfected with expression constructs as indicated. (a–c) Full-length myospryn (a) and minispryn (c) appear to be associated with the internal membranes of the cell when expressed on their own whereas RyR2 (b) labelling is restricted to the endoplasmic reticulum. (d–f) Co-expression of myospryn (d) and RyR2 (e) results in the clustering of both proteins in intensely staining punctae (merged image, f). Note that myospryn is not clustered in the adjacent cell (asterisk) that does express RyR2. (g–i) By contrast co-expression of minispryn (g) and RyR2 (h) does not alter the distribution of either protein (merged image, i). (j – o) Truncated myospryn constructs were used to delineate the regions of the protein involved in RyR2 clustering. MD9 (j) was able to cluster RyR2 (k and merged image, l) whereas the smaller protein MD7 (m) failed to cluster the receptor (n and merged image, o). The underlining denotes the transfected construct for each channel. Scale bar = 10 µm.