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. 2022 Sep 16;13:5445. doi: 10.1038/s41467-022-33108-z

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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 Total AC activity in T. brucei BSF MiTat 1.2 13-90 (parent) or CARP3 RNAi ± 1 μg/mL Tet, 20 h. Mean ± SD of n = 9 (3 independent replicates controlled by Western blot with PFR-A/C as loading control). b Western blot analysis of CARP3 and ESAG4 in T. brucei BSF MiTat 1.2 13-90 (parent) or Tet-induced CARP3 RNAi over 24 h. Signals were normalized to PFR-A/C, parent was set to 100%. c Volcano plot of proteins identified by label-free proteomics in T. brucei BSF MiTat 1.2 13-90 upon CARP3 RNAi ± Tet for 24 h. Proteins are plotted according to p value and fold change. AC isoforms are labeled as blue dots. Protein IDs that differ significantly (two-sided Student’s t test, p value ≤0.05, s₀ = 0.1) in abundance are located above the significance line with their TriTrypDB entries (https://tritrypdb.org) and gene names (in green) indicated. d Analysis of ACP abundance by in-gel fluorescence (C-terminally mNeonGreen tagged ACP1/4/5) or Western blot (C-terminally Ty1 tagged ACP6) in PCF trypanosomes upon CARP3 RNAi ± Tet. CARP3 (anti-CARP3) and ACP signals were normalized to PRF-A/C and day 0 was set to 1; FRDg as loading control. e Cartoon model of the CARP3-AC complex at the membrane including the transmembrane helix and the intracellular parts of an AC dimer (ESAG4). CARP3 N-myristoylation (N-myr) is indicated. The side chains of several basic amino acids of a membrane-proximal helix predicted for CARP3 are shown. A second CARP3 molecule is shown here, as the AC dimer model sterically allows interaction with two CARP3 molecules. f Model illustrating the relative localization of CARP3, AC, FLAM8 and PDEB1 at the anterior tip of the procyclic trypanosome flagellum. Two pools of CARP3 are indicated based on PALM. AC homo- and heterodimerization is indicated by different colors with flagellar tip ACs grouped and colored according to their role in SoMo: ACP1/6 (green) inhibit SoMo, ACP5 (orange) promotes SoMo and ACP3/4 (blue) were not linked to SoMo. Source data to (a, b) and (d) are provided as Source Data file.