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. 2017 Feb;149(2):277–293. doi: 10.1085/jgp.201611721

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© 2017 Yan et al.

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Figure 3. — Na_V1.5 CTD–CaM heterodimer interaction is disrupted by the Y1795C LQT3 mutation. (A and B) Proposed interaction between two Na_V1.5 CTD–CaM heterodimers and position of Y1795C in one of the Na_V1.5 CTDs. The positions of Lys1878 in one Na_V1.5 CTD globular domain (sky blue) and Lys1922 in the IQ domain of a second Na_V1.5 CTD (green), which are available for cross-linking by DSG, are indicated. (C) Coomassie-blue–stained gel of Na_V1.5 CTD and CaM after cross-linking with DSG or buffer control (Con). Molecular weight markers are indicated. (D and F) XMapper display of LC/MS data showing DSG cross-linked peptide 1 for the WT Na_V1.5 CTD and CaM (WT) and the Y1795C mutant Na_V1.5 CTD and CaM. The intensity score (color code) indicates the number of peptides identified for each pairwise interaction. The position of cross-linking between Lys1878 and Lys1922 is circled and indicated by an arrow. (E) LC/MS data showing the cross-linked peptide. (G) Exemplar traces showing increased persistent Na⁺ current for the Y1795C and rescue by CaM overexpression. (H) Quantification of persistent Na⁺ current for the pseudo-WT Na_V1.5^TTX-S and the Y1795C Na_V1.5 mutant with and without CaM overexpression. Data are presented as mean ± SEM. **, P < 0.01.