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. 2018 Aug 2;9:3030. doi: 10.1038/s41467-018-05439-3

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© The Author(s) 2018

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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Fig. 8 — Hypothesized mechanisms by which JNK activation with exercise leads to muscle hypertrophy. Canonical myostatin signaling (depicted with black arrows) results in reduced myofiber size via receptor-mediated phosphorylation of SMAD2 on its C-terminus (Ser465/467). Myostatin-mediated SMAD2 phosphorylation induces dimerization with co-SMAD4 and translocation of the SMAD complex to the nucleus where DNA binding and transcription are initiated. Our data demonstrate that resistance exercise induces JNK activation and phosphorylation of SMAD2 in its linker region via a non-canonical pathway (depicted with red arrows). Phosphorylation of SMAD2 at specific linker region resides (Ser245/250/255) has an inhibitory effect on myostatin activity by preventing the nuclear translocation of SMAD2. Inhibition of myostatin via this novel JNK/SMAD pathway allows for exercise-induced muscle hypertrophy