ArticleThe Journal of biological chemistry2012
A leucine zipper motif essential for gating of hyperpolarization-activated channels.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed, 9 citations in OpenAlex.
- Deletion of Luzp2 Does Not Cause Hearing Loss in Mice.Neuroscience bulletin · 2024Article
- Interplay between VSD, pore, and membrane lipids in electromechanical coupling in HCN channels.eLife · 2023Article
- Identification and Characterization of a Bacterial Homolog of Chloride Intracellular Channel (CLIC) Protein.Scientific reports · 2017Article
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
backgroundIt is poorly understood how hyperpolarization-activated cyclic nucleotide-gated channels (HCNs) function.
resultsWe have identified a leucine zipper in the S5 segment of HCNs, regulating hyperpolarization-activated and instantaneous current components.
conclusionThe 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 is still poorly understood. We have identified a highly conserved leucine zipper motif in the S5 segment of HCN family members. In order to study the role of this motif for channel function, the leucine residues of the zipper were individually mutated to alanine, arginine, or glutamine residues. Leucine zipper mutants traffic to the plasma membrane, but the channels lose their sensitivity to open upon hyperpolarization. Thus, our data indicate that the leucine zipper is an important molecular determinant for hyperpolarization-activated channel gating. Residues of the leucine zipper interact with the adjacent S6 segment of the channel. This interaction is essential for voltage-dependent gating of the channel. The lower part of the leucine zipper, at the intracellular mouth of the channel, is important for stabilizing the closed state. Mutations at these sites increase current amplitudes or result in channels with deficient closing and increased min-P(o). Our data are further supported by homology models of the open and closed state of the HCN2 channel pore. Thus, we conclude that the leucine zipper of HCN channels is a major determinant for hyperpolarization-activated channel gating.
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