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. 2022 Apr 4;13:1787. doi: 10.1038/s41467-022-29503-1

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© The Author(s) 2022

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. 6 — a Schematic representation of TbcrA, TbcrA-RCC1, and TbcrA-TBC. b Proteomic identification of TbcrA as a binding partner of PripA. The table shows the identified unique peptides of TbcrA from PripA-GFP, but not GFP control, pull-down. c Co-immunoprecipitation experiments showing that PripA and PripA-∆PH specifically pulled down TbcrA and TbcrA-RCC1 from cell lysates. Data was from one representative experiment out of two independent experiments. d Co-expression of RFP-tagged PripA, PripA-PH, PripA-∆PH, or VacA with GFP-tagged TbcrA, TbcrA-RCC1, or TbcrA-TBC. The Pearson’s correlation coefficient was 0.94 ± 0.01 for PripA and TbcrA, 0.91 ± 0.03 for PripA and TbcrA-RCC1, 0.24 ± 0.03 for PripA and TbcrA-TBC, 0.33 ± 0.12 for PripA-PH and TbcrA-RCC1, 0.94 ± 0.03 for PripA-ΔPH and TbcrA-RCC1, and 0.09 ± 0.04 for VacA and TbcrA-RCC1. Data represents mean ± SEM (n = 10 cells). The asterisks mark newly formed macropinosomes and the arrows indicate surrounding vesicles. Scale bar = 5 μm. Source data for b, c are provided in this paper.