A leucine zipper motif essential for gating of hyperpolarization-activated channels.

ABSTRACT:

Background

It is poorly understood how hyperpolarization-activated cyclic nucleotide-gated channels (HCNs) function.

Results

We have identified a leucine zipper in the S5 segment of HCNs, regulating hyperpolarization-activated and instantaneous current components.

Conclusion

The leucine zipper is essential for HCN channel gating.

Significance

The identification and functional characterization of the leucine zipper is an important step toward the understanding of HCN channel function. Hyperpolarization-activated cyclic nucleotide-gated (HCN) channels are pacemakers in cardiac myocytes and neurons. Although their membrane topology closely resembles that of voltage-gated K(+) channels, the mechanism of their unique gating behavior in response to hyperpolarization

SUBMITTER: Wemhoner K 

PROVIDER: S-EPMC3504729 | biostudies-literature | 2012 Nov

REPOSITORIES: biostudies-literature