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Ion channels

Shake, rattle or roll?

Nature volume 427, pages 499–500 (2004)Cite this article

Nerve transmission depends on voltage-gated ion-channel proteins, which in turn depend on the behaviour of a membrane domain called the voltage sensor. Therein lies the latest episode in a continuing story.

The propagation of electrical signals in the nervous system endows animals with moment-to-moment overall coherence. Without it, worms could not wriggle, flies could not find fruit, and we could not read News and Views. Electrical impulses coursing down the nerve axon arise from a molecular minuet in which ion-channel proteins deliver charged particles, Na+ and K+, across the nerve membrane. These proteins possess a special property — voltage dependence, not known in any other macromolecule — that causes their activity to be controlled by the very voltage changes they generate. Voltage dependence arises from the transmembrane movement of charged amino acids on the protein, concomitant with opening of the ion-conducting pore. The part of the protein containing these ‘gating charges’, the voltage sensor, is known, but the way it moves is highly controversial. Starace and Bezanilla1 (page 548) now describe a remarkable property of the voltage sensor that sharpens our view of its transmembrane movement.

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Figure 1: Composition of one subunit of a voltage-dependent K+ channel.
Figure 2: Models of voltage-sensor behaviour; the voltage sensors' change from the ‘in’ to the ‘out’ position triggers pore opening.

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Authors and Affiliations

  1. Tufts-New England Medical Center and Department of Neuroscience, Molecular Cardiology Research Institute, Tufts Medical School, 750 Washington Street, Boston, 02111, Massachusetts, USA

    Robert O. Blaustein

  2. Department of Biochemistry, Howard Hughes Medical Institute, Brandeis University, Waltham, 02454, Massachusetts, USA

    Christopher Miller

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  1. Robert O. Blaustein
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  2. Christopher Miller
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Blaustein, R., Miller, C. Shake, rattle or roll?. Nature 427, 499–500 (2004). https://doi.org/10.1038/427499a

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