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. 2008 Dec 15;183(6):1101–1114. doi: 10.1083/jcb.200805169

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© 2008 Bréchet et al.

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.jcb.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).

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Figure 6. — Impact of K_v2.1-Na_v1.2 and of phosphorylation-deficient K_v2.1-Na_v1.2 constructs on the accumulation of sodium channels (Na_v1) and KCNQ2/KCNQ3 potassium channels at the AIS of cultured hippocampal neurons. (A, top and middle) K_v2.1-Na_v1.2 expression perturbed Na_v1 accumulation at the AIS, unlike the phosphorylation-deficient K_v2.1-Na_v1.2 4SA mutant. Hippocampal neurons were transfected with either K_v2.1-Na_v1.2 or phosphorylation-deficient K_v2.1-Na_v1.2 mutants. Then cells were stained for myc (gray), ankyrin G (red), and sodium channels (green). (B) Quantification of Na_v1 and ankyrin G staining intensity in untransfected cells (A, open arrowheads) and in transfected cells (closed arrowheads). (A, bottom) K_v2.1-Na_v1.2 expression did not perturb KCNQ3 accumulation at the AIS. Cells transfected with K_v2.1-Na_v1.2 were subsequently stained for myc (gray), ankyrin G (red), and KCNQ3 potassium channels (green). (C) Quantification of KCNQ3 and ankyrin G staining intensity. Fluorescence intensity measured in transfected cells, identified by myc staining, was normalized by taking as 100% the staining intensity measured in nontransfected cells (arrowheads). Numbers at the base of the bars denote the number of quantified cells. Error bars indicate mean ± SEM. Mann-Whitney test: *, P < 0.05; **, P < 0.01; ***, P < 0.001. WT, wild type. Bars, 10 μm.