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. 2017 Nov 1;8:1237. doi: 10.1038/s41467-017-01437-z

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© The Author(s) 2017

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. 7 — A model of F₁F₀-ATP synthase assembly. After insertion into the inner mitochondrial membrane, Atp6 associates with Atp10 and Atp23 and undergoes N-terminal processing (state 1). Moreover, Atp6 interacts with Atp8 to form an early assembly intermediate, which consists of Atp6, Atp8, Atp10, and Atp23–Atp6/8 module (state 2). Presumably, the Atp6/8 module serves as an assembly platform for the peripheral stalk and F₁ (state 3). Moreover, the INA complex associates with this later assembly intermediate and, most likely, keeps it in a primed state for Atp9 oligomer association. In addition, the INA complex interacts with the Atp9 oligomer and facilitates formation of the proton-conducting channel in the last step of F₁F₀-ATP synthase assembly (step 4). After the last assembly step, assembly factors are released and recycled (step 5)