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. 2024 Sep 27;15:8390. doi: 10.1038/s41467-024-52703-w

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© The Author(s) 2024

Open Access This article is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License, which permits any non-commercial use, sharing, 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 licence, and indicate if you modified the licensed material. You do not have permission under this licence to share adapted material derived from this article or parts of it. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by-nc-nd/4.0/.

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Fig. 6 — Top panel: rat liver perfusion experiments reveal the time resolved glucagon-regulated phosphoproteome to identify vesicle trafficking and SEC22B as potential players. Middle panel: molecular physiology experiments reveal that hepatic SEC22B and SEC22B-S137 phosphorylation are required for glucagon-regulated metabolism. Bottom panel: hepatic SEC22B interactome experiments unveil mechanisms by which SEC22B and S137 phosphorylation may regulate metabolism downstream of glucagon. Created in BioRender. Wu, Y. (2023) BioRender.com/j53f752.