Fig. 3: DNRX physically interacts with DG through its extracellular domain. | Communications Biology

Fig. 3: DNRX physically interacts with DG through its extracellular domain.

From: Neurexin facilitates glycosylation of Dystroglycan to sustain muscle architecture and function in Drosophila

Fig. 3

a Coimmunoprecipitation demonstrating the interaction between DNRX and DG in Drosophila muscle. An anti-GFP antibody was used to label DNRX, and an anti-HA antibody was used to label DG. Left: Immunoprecipitation with an anti-HA antibody. Right: Immunoprecipitation with an anti-GFP antibody. b Construction of plasmids with deletion of different regions of DNRX and the Dg-C isoform. c Coimmunoprecipitation demonstrating that DNRX interacts with DG through its extracellular region in S2 cells. An anti-GFP antibody was used for immunoprecipitation. d Coimmunoprecipitation demonstrating that DG interacts with DNRX through its extracellular region in S2 cells. An anti-mCherry antibody was used for immunoprecipitation. e Coimmunoprecipitation demonstrating that DNRX interacts with multiple regions of Dg-C in S2 cells. An anti-mCherry antibody was used for immunoprecipitation.

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