Site-directed mutagenesis identified a region near the amino terminus of the Shaker potassium channel that forms a cytoplasmic domain interacting with the open channel to cause inactivation.
Identifies a specific amino-terminal region in Shaker potassium channels that acts as a cytoplasmic domain to cause channel inactivation.
The potassium channels encoded by the Drosophila Shaker gene activate and inactivate rapidly when the membrane potential becomes more positive. Site-directed mutagenesis and single-channel patch-clamp recording were used to explore the molecular transitions that underlie inactivation in Shaker potassium channels expressed in Xenopus oocytes. A region near the amino terminus with an important role in inactivation has now been identified. The results suggest a model where this region forms a cytoplasmic domain that interacts with the open channel to cause inactivation.
Hoshi et al. (Fri,) conducted a other in Shaker potassium channel inactivation. Site-directed mutagenesis was evaluated on Molecular transitions underlying inactivation. Site-directed mutagenesis identified a region near the amino terminus of the Shaker potassium channel that forms a cytoplasmic domain interacting with the open channel to cause inactivation.