Skip to main content
. 2022 Feb 9;41(12):1821–1834. doi: 10.1038/s41388-022-02212-1

Fig. 2. DDR1 physically interacts and colocalized with ARF6.

Fig. 2

A Cellular extracts from SK-Hep1 and HLF cells transfected with FLAG-tagged DDR1 or FLAG-tagged vector were subsequently immunoprecipitated with anti-FLAG antibody. Eluted proteins were separated on SDS-PAGE and visualized by Coomassie blue staining. Eluted proteins were identified by mass spectrometry analysis. B Selective genes from mass spectrometry analysis were co-immunoprecipitated with Myc-tagged DDR1 (up). Detection of ARF6 by mass spectrometry (bottom). C 293 T cells were transiently co-transfected with indicated plasmids and co-immunoprecipitation assays were performed. D Immunoblots of co-immunoprecipitated (IP) endogenous DDR1 and endogenous ARF6 in HLE cell extracts. Immunoglobulin G (IgG) is negative control. E Confocal assays were shown to observe the co-localization of exogenously expressed DDR1 and ARF6 in 293 T cells (Scale bar: 15 μm). F Confocal assays were shown to observe the co-localization of endogenous DDR1 and ARF6 in HLF and HLE cells (Scale bar: 30 μm). G Schematic diagram of FLAG-tagged full-length or deletion constructs of ARF6 used in this study (left panel). Co-precipitation of HA-tagged DDR1 with FLAG-tagged ARF6 or its mutants, analyzed by anti-FLAG immunoprecipitation and anti-FLAG/ HA immunoblots (right panel).