The voltage-gated potassium channels and their relatives

@article{Yellen2002TheVP,
  title={The voltage-gated potassium channels and their relatives},
  author={Gary Yellen},
  journal={Nature},
  year={2002},
  volume={419},
  pages={35-42}
}
  • G. Yellen
  • Published 5 September 2002
  • Biology
  • Nature
The voltage-gated potassium channels are the prototypical members of a family of membrane signalling proteins. These protein-based machines have pores that pass millions of ions per second across the membrane with astonishing selectivity, and their gates snap open and shut in milliseconds as they sense changes in voltage or ligand concentration. The architectural modules and functional components of these sophisticated signalling molecules are becoming clear, but some important links remain to… 
Thermodynamics of voltage-gated ion channels
TLDR
The thermodynamic mechanisms of the VGIC superfamily are discussed, including the two-state gating mechanism, sliding-rocking mechanism of the voltage sensor, subunit cooperation, lipid-infiltration mechanism of inactivation, and the relationship with their structural features.
Polyamine Block of Kir Channels
TLDR
In the context of biophysical studies of ion channels, this term is used to describe a voltage dependence of macroscopic currents in which currents through an ion channel flow preferentially into the cell or out of the cell.
Functional diversity of potassium channel voltage-sensing domains
TLDR
Differences in detailed VSD functioning among voltage-gated potassium channels might have physiological consequences that have not been explored and which might reflect evolutionary adaptations to the different roles played by Kv channels in cell physiology.
Gating of two-pore domain K+ channels by extracellular pH.
TLDR
This work discusses the mechanism for this gating in terms of electrostatic effects on the pore changing the occupancy and open probability of the channels in a way reminiscent of C-type inactivation gating at the selectivity filter.
Cytoplasmic Domains and Voltage-Dependent Potassium Channel Gating
TLDR
The present knowledge about the molecular organization of these intracellular channel regions and their role in both setting and controlling Kv voltage-dependent gating properties are reviewed.
Gating the pore of P2X receptor channels
TLDR
The results show that TM2 lines the central ion-conduction pore, TM1 is positioned peripheral to TM2 and the flow of ions is minimized in the closed state by a gate formed by the external region of TM2.
Heteroligomeric interactions of the Kv1.3 channelosome
TLDR
This thesis deciphered the molecular mechanisms involved in this effect concluding a bipartite system: masking of Kv1.3 export signal and transference of a retention signal to the channelosome.
BK channel activation: structural and functional insights
The Domain and Conformational Organization in Potassium Voltage-Gated Ion Channels
TLDR
In this review, the recent data about domain organization of eukaryotic potassium voltage-gated ion channels is shown, giving special attention to the interaction between the domains and the corresponding conformational changes upon activation of the channel.
Voltage-dependent gating of KCNH potassium channels lacking a covalent link between voltage-sensing and pore domains
TLDR
It is shown that truncated proteins interrupted at, or lacking the S4–S5 linker produce voltage-gated channels in a heterologous model that recapitulate both the voltage-sensing and permeation properties of the complete protein.
...
...

References

SHOWING 1-10 OF 99 REFERENCES
Voltage gating of ion channels.
TLDR
Voltage-gated sodium channels initiate the nerve action potential and provide for its rapid propagation because the ion fluxes through these channels regeneratively cause more channels to open.
A Prokaryotic Voltage-Gated Sodium Channel
TLDR
The identification of NaChBac as a functionally expressed bacterial voltage-sensitive ion-selective channel provides insight into both voltage-dependent activation and divalent cation selectivity.
Voltage-dependent gating of sodium channels: correlating structure and function
Crystal structure and mechanism of a calcium-gated potassium channel
TLDR
This work has cloned, expressed, analysed electrical properties, and determined the crystal structure of a K+ channel (MthK) from Methanobacterium thermoautotrophicum in the Ca2+-bound, opened state.
Structure of a Voltage-Dependent K+ Channel β Subunit
Structure of a voltage-dependent K+ channel beta subunit.
TLDR
The structure of the conserved core of mammalian beta subunits is determined by X-ray crystallography at 2.8 A resolution and suggests a mechanism for coupling membrane electrical excitability directly to chemistry of the cell.
The open pore conformation of potassium channels
TLDR
Amino-acid sequence conservation suggests a common structural basis for gating in a wide range of K+ channels, both ligand- and voltage-gated.
Blocker protection in the pore of a voltage-gated K+ channel and its structural implications
TLDR
The ability of blockers to protect against chemical modification of cysteines introduced at sites in transmembrane segment S6, which contributes to the intracellular entrance, is investigated.
A functional connection between the pores of distantly related ion channels as revealed by mutant K+ channels.
TLDR
It is demonstrated that very small differences in the primary structure of an ion channel can account for extreme functional diversity, and they suggest a possible connection between the pore-forming regions of K+, Ca2+, and cyclic nucleotide-gated ion channels.
...
...