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
  • Chemistry, Medicine
  • 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… Expand
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615 Citations
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615 Citations

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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. Expand
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Heteroligomeric interactions of the Kv1.3 channelosome
Voltage-gated potassium channels are proteins that allow the flux of potassium ions across the plasma membrane in response to a voltage stimulus. Kv1.3 is expressed at the immune system and it has… Expand
BK channel activation: structural and functional insights
  • U. Lee, J. Cui
  • Chemistry, Medicine
  • Trends in Neurosciences
  • 2010
TLDR
Recently published electron cryomicroscopy and X-ray crystallographic structures of the BK channel provided the first glimpse into the assembly of these domains, corroborating the close interactions among these domains during channel gating that have been suggested by functional studies. Expand
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. Expand
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