Fig. 1: SNX17 uses its C-terminal tail to bind Retriever. | Nature Communications

Fig. 1: SNX17 uses its C-terminal tail to bind Retriever.

From: Structural basis for Retriever-SNX17 assembly and endosomal sorting

Fig. 1

a Cartoon depiction of Retriever and the domain architecture of SNX17. b Cartoon representation of GST-SNX17 constructs used (left panel) and Coomassie blue-stained SDS PAGE gels showing in vitro GST pull-down between indicated GST-SNX17 constructs and Retriever (right panel). c Coomassie blue-stained SDS PAGE gels showing in vitro GST pull-down between GST-SNX17 and Retriever in the presence of increasing concentrations of a competing peptide consisting of the last 20 amino acids of SNX17. d Binding isotherms obtained from EPD assays measuring the binding affinity between GST-SNX17 CT and Retriever. Data were pooled from three independent experiments and globally fitted to a one-binding site model to obtain the KD and fitting error48. GST pull-down as a negative control was from one experiment. Representative Coomassie blue-stained SDS-PAGE gels from the EPD experiments are shown in Supplementary Fig. 1a. Coomassie blue-stained SDS PAGE gels showing in vitro GST pull-down between GST-SNX17, and Retriever complexed with CCDC22-CCDC93 VBD dimer (e) or isolated subunits of Retriever (f). Representative results from at least two independent experiments are shown for each pull-down. Source data for b–f are provided as a Source Data file.

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