Fig. 5: Mutations at the interface between Arl1 and Gea2 affect their interaction.
From: Structural insight into an Arl1–ArfGEF complex involved in Golgi recruitment of a GRIP-domain golgin
a As a control, deletion of Gea2 DCB domain abolished Arl1–Gea2 interaction. Individually mutating the Arl1-specific residues L69 and Y78 significantly reduced Arl1 binding to Gea2 and Arl1 L69A, Y78L double mutation abolished Arl1–Gea2 interaction. 3xFLAG tagged WT Gea2 or Gea2 mutant variants were co-expressed with 3xHA tagged WT Arl1 or Arl1 mutant variants in gea2∆arl1∆ cells. Gea2-3xFLAG was immunoprecipitated by anti-FLAG M2 magnetic beads, and the coprecipitated Arl1-3xHA was detected with anti-HA antibody. b Quantification of coprecipitated Arl1 (n = 3). Comparisons were calculated via a One-Way ANOVA followed by Dunnett’s multiple comparisons test. n = 3 represents data from three independent biological replicates. Error bars represent SD. *** indicates p value < 0.001. Source data are provided as a Source Data file.
