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. 2018 Nov 5;9:4624. doi: 10.1038/s41467-018-06853-3

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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 — A model for H19-mediated regulation of 4E-BP1 phosphorylation. When H19 is abundant (right panel), mTORC1 activity is attenuated because H19 inhibits 4E-BP1 phosphorylation by disrupting the interaction between 4E-BP1 and Raptor. The reduced 4E-BP1 phosphorylation allows 4E-BP1 to bind elF4E, thus inhibiting its protein translation function. When H19 is absent, 4E-BP1 binds to Raptor and thus is more readily and effectively phosphorylated. This prevents its interaction with elF4E, resulting in increased protein translation