Neuron
ArticleA peptide segment critical for sodium channel inactivation functions as an inactivation gate in a potassium channel
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Cited by (44)
Structure of the Na<inf>v</inf>1.4-β1 Complex from Electric Eel
2017, CellCitation Excerpt :Nav channels inactivate by both fast and slow mechanisms (Ahern et al., 2016; Ulbricht, 2005). The IFM motif on the III-IV linker was characterized to be critical for fast inactivation (Patton et al., 1993; Stühmer et al., 1989; Vassilev et al., 1989; West et al., 1992), and a number of residues on S4-S5 and S6 segments in repeats III and IV were shown to be involved in this process (McPhee et al., 1995, 1998; Smith and Goldin, 1997; Tang et al., 1996). In the structures of NavPaS and Cav1.1, a conserved helix on the III-IV linker interacts with the CTD, but neither channel contains the IFM motif (Shen et al., 2017; Wu et al., 2016).
Competitive and non-competitive regulation of calcium-dependent inactivation in Ca<inf>V</inf>1.2 L-type Ca<sup>2+</sup> channels by calmodulin and Ca<sup>2+</sup>-binding protein 1
2013, Journal of Biological ChemistryCitation Excerpt :Multiple molecular determinants for inactivation have been identified. However, unlike for some voltage-dependent K+ and Na+ channels (4), the dynamics of conformational changes that culminate in VDI and CDI are controversial and remain the subject of intense research (5–10). CaM and CaBP1 are members of a large family of Ca2+ sensors and regulators that diversify Ca2+ signaling and neuronal activity through VGCCs and other pathways (11).
Fibroblast Growth Factor Homologous Factors Control Neuronal Excitability through Modulation of Voltage-Gated Sodium Channels
2007, NeuronCitation Excerpt :Mathematical modeling suggests that alterations in the rate constants governing the transition from closed and open states into the inactivated states is sufficient to cause the electrophysiological changes observed in Fhf1−/−Fhf4−/− mice. Sodium channel inactivation is governed by interaction between an inactivation “particle” housed in the III-IV cytoplasmic loop and the inner pore of the channel (Patton et al., 1993; Vassilev et al., 1988; West et al., 1992). The channel C-terminal tail also contributes to inactivation (An et al., 1998; Glaaser et al., 2006; Mantegazza et al., 2001), potentially through contacts between the tail and the III-IV loop (Motoike et al., 2004).
Block of inactivation-deficient cardiac Na<sup>+</sup> channels by acetyl-KIFMK-amide
2005, Biochemical and Biophysical Research CommunicationsCitation Excerpt :Despite these uncertainties, it is worth noting that the block of the Na+ channel by acetyl-KIFMK amide is quite similar to the action of the inactivation peptide in K+ channels responsible for the N-type fast inactivation process [22]. A transposed Na+ channel D3–D4 linker also acts as an inactivation gate in chimeric K+ channels, suggesting a functional relationship between fast inactivation process of Na+ and K+ channels [23]. The open Na+ channel may have an entryway of ∼15 Å in diameter toward the inner cavity [24].
A model of voltage gating developed using the KvAP channel crystal structure
2004, Biophysical JournalCitation Excerpt :In Shaker channels, residues in the latter portion of S1 and S3, in the initial part of S2 and S4, and in the S1-S2 and S3-S4 loops are accessible from the extracellular solution in all conformations (Gandhi et al., 2003) (analogous KvAP residues in Structure 1 are located on or near the opposite side of the membrane). Residues immediately preceding S1 in Shaker channels are located in the cytoplasm (Patton et al., 1993) (in Structure 1 analogous KvAP residues are in the center of the transmembrane region). Except for the S3-S4 hairpin, the tertiary structure of the voltage-sensing domain in Structure 1 deviates substantially from the crystal structure (see Fig. 2 B) of the isolated KvAP voltage-sensing domain, Structure 2 (Jiang et al., 2003a).
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Present address: Department of Physiology, UCLA School of Medicine, Los Angeles, California 90024.
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Present address: Cell Therapeutics Inc., Seattle, Washington 98102.