Fig. 5: CARP3 interacts with ACs.
From: A multi-adenylate cyclase regulator at the flagellar tip controls African trypanosome transmission
Volcano plot representation of proteins identified upon GFP trap pull-down in T. brucei AnTat 1.1E CARP3-YFP cells compared to wild type (WT) in BSFs (a) or PCFs (b) (n = 2 replicate pull-downs each). Identified proteins are plotted according to p value and fold change with significantly enriched proteins (p value ≤0.05, fold change ≥10) shown in blue with their TriTrypDB entries (https://tritrypdb.org). The bait protein CARP3 and AC isoforms are indicated in green. c CARP3 immunoprecipitation (anti-CARP3 coupled to protein A beads) in BSF cell lines expressing ESAG4-GFP, ESAG4∆c107-GFP, or ESAG4∆CAT-GFP, respectively. Pull-down assays in a PKAR-GFP cell line served as negative control. Upper panels: detection of GFP by in-gel fluorescence; lower panels: Western blot detection of CARP3. The asterisk labels the fluorescent band corresponding to the respective GFP fusion protein. IN input; FT flow-through; E elution (10x load of input or flow-through); M protein molecular weight marker. d CARP3 immunoprecipitation (anti-CARP3 coupled to protein A beads) from soluble fractions of HEK293 cells expressing CARP3 or ESAG4-2Ty1 or both. Equal amounts of total DNA were transfected in all conditions (ratio of transfected plasmids 1:1). The upper Western blot was probed with anti-Ty1, the lower with anti-CARP3. IN soluble input, P insoluble pellet, FT flow-through, E elution, M protein molecular weight marker, HC anti-CARP3 heavy chain, LC anti-CARP3 light chain. Source data to (c) is provided as Source Data file.
