Key result
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.
Hypothesis-generating for K+ channel gating; leaves open conservation and therapeutic targeting in human Kv homologs.
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.
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Hoshi et al. (1990) studied 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.
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