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. 2008 Aug 11;182(3):573–585. doi: 10.1083/jcb.200802164

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© 2008 Han 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 7. — CaMKIα-dependent phosphorylation regulates Drp1 intracellular distribution in neurons. (A) Neurons (10 DIV) were transfected with YFP-Drp1 or YFP-Drp1-S600A. Neurons (at 11 DIV) were untreated (left) or treated with (right) 45 mM K⁺ or preincubated with 20 μM KN93 for 30 min before high K⁺ stimulation. Bars, 10 μm. (B) Quantitative analysis of exogenous Drp1 foci. Data were obtained from at least five independent experiments for each condition shown in A. Control is YFP-Drp1 without stimulation. Error bars indicate SD in each group. *, P < 0.05. (C) Neurons were treated with 45 mM K⁺ in the absence or presence of 20 μM KN93 for various times as indicated. Proteins in mitochondrial fractions were separated by SDS-PAGE and analyzed by immunoblotting using Drp1 T-Drp1, P-Drp1, or Tom40 (for quantification of mitochondrial membrane) antibodies. (D) Quantitative analysis of Drp1 translocation. Drp1 levels were normalized to Tom40 levels at the time points indicated in Fig. 7 C. Cumulative results from three independent experiments for each condition are shown. Error bars indicate the mean ± SEM in each group.