Fig. 1
From: γ-2 and GSG1L bind with comparable affinities to the tetrameric GluA1 core
Assembly of GluA1-tdCherry with GSG1L-GFP. A On a single-molecule level, GluA1-tdCherry tetramers appear as bright spots in the Xenopus oocyte membrane. Tracking their position (inset) suggests that they are immobile. B In contrast, GSG1L-GFP spots have a higher mobility. C When coexpressed, GluA1-tdCherry (red) and GSG1L-GFP (green) colocalized, and the latter became immobile. D The intensity of an individual spot where GluA1-tdCherry and GSG1L-GFP colocalized. Bars above the trace indicate emission in the respective channel. While in the GFP channel, individual photobleaching steps can be identified, the tdCherry emission appears as a decay without individual steps. E GSG1L-GFP photobleaching steps in the colocalizing spots. F Correction for non-fluorescent GFP suggests that up to 4 GSG1L-GFP can bind to each GluA1-tdCherry core. Scale bars 2 µm and 1 µm (insert)