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. 2024 Jan 17;25(2):813–831. doi: 10.1038/s44319-023-00055-9

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© The Author(s) 2024

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 licence, and indicate if changes were made. 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/4.0/. Creative Commons Public Domain Dedication waiver http://creativecommons.org/publicdomain/zero/1.0/ applies to the data associated with this article, unless otherwise stated in a credit line to the data, but does not extend to the graphical or creative elements of illustrations, charts, or figures. This waiver removes legal barriers to the re-use and mining of research data. According to standard scholarly practice, it is recommended to provide appropriate citation and attribution whenever technically possible.

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Under nutrient-rich conditions (left panel), TORC1-dependent phosphorylation prevents the tight association of Atg13 with Atg17 and Atg1, preventing the initiation of bulk autophagy. When starvation occurs (right panel), TORC1 activity is inhibited, leading to the dephosphorylation of Atg13. Dephosphorylated Atg13 exhibits increased affinity for Atg17 and Atg1, serving as a switch that triggers the phase separation of the PAS. The phase-separated condensate is formed by numerous multivalent interactions involving Atg13, the Atg17 complex, Atg1, and Atg11. Consequently, Atg13 acts as a signaling hub, with its phosphorylation status regulating the level of bulk autophagy activity and allowing precise control over the process.