Fig. 6. In vitro interactions of plectin 1 with -dystrobrevin and β-synemin. (A) -Dystrobrevin fragments (-Dbr, 0.8 µg) were incubated with GST-fused β-synemin (β-Syn, 10 µg) or GST (1.8 µg) in the incubation buffer (1 ml) and then precipitated by glutathione beads (Gl-beads, 50 µl). GST-fused β-Syn precipitated -Dbr, but GST alone did not. (B) -Dbr (0.5 µg) were incubated with Myc-tagged plectin 1 (PleN1, 9.6 µg) or plectin 1f fragments (PleN1f, 3.2 µg) or β-galactosidase (LacZ, 7.6 µg) in the incubation buffer (1.4 ml) including 0.4% BSA and then immunoprecipitated with anti-Myc antibody (4 µg) and protein L-agarose (40 µl). PleN1 coimmunoprecipitated with -Dbr, but neither PleN1f nor LacZ did. (C) -Dbr (0.4 µg) and GST-fused β-Syn (2 µg)were incubated with Myc-tagged PleN1 (9 µg) or PleN1f (3 µg) or LacZ (9 µg) in the incubation buffer (1.2 ml) including 0.4% BSA and then immunoprecipitated with anti-Myc antibody (4 µg) and protein L-agarose (40 µl). PleN1 coimmunoprecipitated with both β-Syn and -Dbr, whereas PleN1f pulled down only β-Syn. However, LacZ and PleN1 in combination with control IgG pulled down none of them.