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| Content Provider | Springer Nature Link |
|---|---|
| Author | Peña, Pilar Machín, Angeles Fernández Trillo, Jorge Domínguez, Pedro Barros, Francisco |
| Copyright Year | 2014 |
| Abstract | The N-terminal-most N-tail of the human ether-à-go-go-related gene (hERG) potassium channel is a crucial modulator of deactivation through its interactions with the S4-S5 loop and/or the C-linker/cNBD, leading to a stabilization of the channel’s open state. Not only the N-terminal, but also the initial C-terminal region of the channel can modulate the transitions between the open and closed states either by direct or by indirect/allosteric interactions with the gating machinery. However, while a physical proximity of the N-tail to the gating machinery has been demonstrated in the closed state, data about their possible interaction in other channel conformations have been lacking. Using a site-directed cysteine mutagenesis and disulfide chemistry approach, we present here evidence that a physical proximity between the N-tail and the gating-related structures can also exist in channels held between pulses in the open/inactive state, highlighting the physiological and functional relevance of the direct interactions between the N-terminal tail and the S4-S5 loop and/or C-linker structures for modulation of channel. |
| Starting Page | 1747 |
| Ending Page | 1756 |
| Page Count | 10 |
| File Format | |
| ISSN | 00316768 |
| Journal | Pflügers Archiv |
| Volume Number | 467 |
| Issue Number | 8 |
| e-ISSN | 14322013 |
| Language | English |
| Publisher | Springer Berlin Heidelberg |
| Publisher Date | 2014-09-17 |
| Publisher Place | Berlin, Heidelberg |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Potassium channel Ether-à-go-go-related gene Disulfide bridging Structure-function relationship Cytoplasmic domains Gating modulation Human Physiology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Physiology Physiology (medical) Clinical Biochemistry |
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