NEUROSCIENCE. For the article “Fluorometric measurements of conformational changes in glutamate transporters,” by H. Peter Larsson, Anastassios V. Tzingounis, Hans P. Koch, and Michael P. Kavanaugh, which appeared in issue 11, March 16, 2004, of Proc. Natl. Acad. Sci. USA (101, 3951-3956; first published March 4, 2004; 10.1073/pnas.0306737101), the authors note that, due to a typographical error, several of the rates in Fig. 4A are incorrect. The corrected figure and its legend appear below.
Fig. 4.
An EAAT3 model with only three conformational changes simulates our experimental findings. (A) A modified 15-state model (16, 28) used to simulate the fluorescence data. The steady-state fluorescence data are well described by the 15-state model, after assigning three fluorescence intensities (2.4, 1.24, and -4) to the different states indicated by the dashed boxes. (B) Simulation of ΔF-V in different external solutions: 100 mM Na+ (○), 100 mM choline (□), 100 mM K+ (▵), and 100 Na+ mM plus 1 mM glutamate (⋄). (C) Simulation of ΔF-V in different external Na+ concentrations: 50 mM (○), 100 mM (▵), 200 mM (□) (pHexternal 7.5). (D) Simulation of ΔF-V at different external pH: pH 6.5 (□), pH 7.5 (⋄), and pH 8.5 (○); Na+external = 100 mM. (E) Simulated reverse transport current. The steady-state reverse transport current at 0 mV is plotted at different pH (both internal and external were altered in parallel): K+internal = 50 mM, K+external = 50 mM, Na+internal = 25 mM, Na+external = 25 mM, glutamateinternal = 10 mM, and glutamateexternal = 0.1 μM.