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. 2018 Nov 22;8:36. doi: 10.1186/s13395-018-0182-x

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© The Author(s). 2018

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided 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 Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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Fig. 5 — The model of sarcolemmal nNOS restoration by R16/17-Syn PDZ fusion protein. The R16/17-Syn PDZ fusion protein is targeted to the sarcolemma by the membrane-targeting motif (Pal). R16/17 and the syntrophin PDZ domain in the fusion protein interact with nNOSμ PDZ domain to anchor nNOSμ to the sarcolemma (not drawn to scale). Please note an activated nNOSμ exists as a dimer. It is currently unclear how exactly the two PDZ domains in the nNOSμ dimer interact with dystrophin R16/17 and the syntrophin PDZ domain. It is possible that one nNOSμ PDZ domain interacts with dystrophin R16/17 and the other nNOSμ PDZ domain interacts with the syntrophin PDZ domain. It is also possible that a single nNOSμ PDZ domain can interact with both dystrophin R16/17 and the syntrophin PDZ domain. For simplicity, the activated nNOSμ dimer was depicted as a single molecule in this cartoon