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Published Erratum
. 2015 Dec;146(6):541-6.
doi: 10.1085/jgp.20121093510232015c. Epub 2015 Nov 16.

Correction: S1-S3 counter charges in the voltage sensor module of a mammalian sodium channel regulate fast inactivation

James R Groome, Vern Winston
Published Erratum

Correction: S1-S3 counter charges in the voltage sensor module of a mammalian sodium channel regulate fast inactivation

James R Groome et al. J Gen Physiol. 2015 Dec.
No abstract available

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Figures

Figure 2.
Figure 2.
Conductance in hNaV1.4 and ENC mutations. (A) Traces for wild-type and mutant channels in response to depolarizing commands to voltages ranging from −90 to 60 mV. I-V relations are shown for ENC mutations in domains I and II (B), domain III (C), and domain IV (D). Values represent mean ± SEM (error bars) from 10–22 experiments. Additional panels are shown for g-V relations in domains I and II (E), domain III (F), and domain IV (G). Boltzmann fits to each plot are shown by dotted lines.
Figure 6.
Figure 6.
Activation parameters for mutations at S1 HCR locus in hNaV1.4. (A) Traces shown are responses to depolarization to 0, 20, 40, and 60 mV for mutations in domains I–III. Plots in B, D, and F show I-V relations for mutations in these domains; plots in C, E, and G show activation kinetics. Values represent mean ± SEM (error bars) from 11–24 experiments. Additional panels are shown for g-V relations for hNaV1.4 and mutations of the HCR in domain I (H), domain II (I), and domain III (J). Boltzmann fits to each plot are shown by dotted lines.
Figure 10.
Figure 10.
Biophysical characterization of INC mutations. (A) Sodium currents in response to command depolarization to voltages from −90 to 60 mV. Effects of INC mutations are shown for activation (B), steady-state fast inactivation (C), entry into fast inactivation (D and E), and recovery (F and G). Legends identify residues and locus by domain and segment. Values represent mean ± SEM (error bars) from 10–23 experiments. The additional panel (H) is shown for g-V relations for hNaV1.4 and mutations of the INC in domains I and II. Boltzmann fits to each plot are shown by dotted lines.
Figure 11.
Figure 11.
Three-dimensional plot showing the effect of charge-reversing mutations of residues in ENC (green), HCR (red), and INC (blue) regions. Shown for each domain are shifts in inactivation kinetics at 20 mV (x axis), activation probability (y axis), and inactivation probability (z axis). Corrected values for V0.5 shifts shown in B are calculated from g-V relations of Table 3.
See this image and copyright information in PMC

Erratum for

References

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    1. DeCaen P.G., Yarov-Yarovoy V., Scheuer T., and Catterall W.A.. 2011. Gating charge interactions with the S1 segment during activation of a Na+ channel voltage sensor. Proc. Natl. Acad. Sci. USA. 108:18825–18830. 10.1073/pnas.1116449108 - DOI - PMC - PubMed
    1. Pless S.A., Elstone F.D., Niciforovic A.P., Galpin J.D., Yang R., Kurata H.T., and Ahern C.A.. 2014. Asymmetric functional contributions of acidic and aromatic side chains in sodium channel voltage-sensor domains. J. Gen. Physiol. 143:645–656. 10.1085/jgp.201311036 - DOI - PMC - PubMed

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