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. 2021 Jun 18;12:3788. doi: 10.1038/s41467-021-24083-y

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© The Author(s) 2021

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. 10 — Left: in the endosome-like compartment (ELC) where protein trafficking to secretory organelles is determined, Asp3 protease cleaves the N-terminal transmembrane segment of RON13. Rhoptry proteins, including RONs and ROPs (violet tones), are phosphorylated by RON13 within this compartment. Center: RON13-phosphorylated proteins assemble to form the RON complex within the rhoptry neck, prior to being secreted into the host. Right: the RON complex, localized to the cytosolic face of the host, contributes to parasite invasion by forming a moving junction by associating with adhesins at the parasite plasma membrane (blue). Phosphorylated proteins of the RON complex additionally recruit host proteins (green) to assist in parasite invasion and subvert host cellular functions.