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Figure 7


Fig. 7. The ankyrin-G-interaction domain mediates retention of KCNQ2/3 complexes at the AIS. (A) Hippocampal neurons were co-transfected with hKCNQ2-delAnkG ({Delta}803-844) (hQ2-delAnkG) + hKCNQ3-FLAG (hQ3), hKCNQ2-cmyc (hQ2-cmyc) + hKCNQ3-delAnkG ({Delta}826-872) (hQ3-delAnkG), hKCNQ2-delAnkG + hKCNQ3-delAnkG, or KCNQ2-E810A/S811A/D812A (KCNQ2-AAA) and KCNQ3-E837A/T838A/D839A (KCNQ3-AAA). The cells were fixed and triple-labeled for hKCNQ2, hKCNQ3 and ankyrin-G. Bar, 20 µm. hKCNQ2-delAnkG/hKCNQ3-FLAG were enriched at the AIS to the same extent as wild-type hKCNQ2/hKCNQ3. For hKCNQ2-cmyc/hKCNQ3-delAnkG complexes a significant reduction in the AIS enrichment was observed (see also Fig. 5). For hKCNQ2-delAnkG/hKCNQ3-delAnkG and hKCNQ2-AAA/hKCNQ3-AAA complexes AIS enrichment was abolished. (B) Representative current traces of a hKCNQ2-delAnkG/hKCNQ3-delAnkG transfected neuron in the absence or presence of 10 µM XE-991. Protocols were as described in Fig. 2. Current levels were comparable with those observed for full-length KCNQ2-cmyc/KCNQ3-FLAG transfected neurons, thus the hKCNQ2-delAnkG/hKCNQ3-delAnkG complex is still trafficked to the cell surface.





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