ArticleThe Journal of biological chemistry2011
Tissue-specific N terminus of the HCN4 channel affects channel activation.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- The proximal N-terminus of IRAG is required for potentiation of HCN4 channels.bioRxiv : the preprint server for biology · 2026Article
- LRMP inhibits cAMP potentiation of HCN4 channels by disrupting intramolecular signal transduction.eLife · 2024Article
- LRMP inhibits cAMP potentiation of HCN4 channels by disrupting intramolecular signal transduction.bioRxiv : the preprint server for biology · 2024Article
- Palmitoylation regulates the magnitude of HCN4-mediated currents in mammalian cells.Frontiers in physiology · 2023Article
- Isoform-specific regulation of HCN4 channels by a family of endoplasmic reticulum proteins.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- New Structures and Gating of Voltage-Dependent Potassium (Kv) Channels and Their Relatives: A Multi-Domain and Dynamic Question.International journal of molecular sciences · 2019Review
- Cellular context and multiple channel domains determine cAMP sensitivity of HCN4 channels: ligand-independent relief of autoinhibition in HCN4.The Journal of general physiology · 2012Article
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hyperpolarization-activated cyclic nucleotide-gated (HCN) channels are expressed in the brain and heart and are essential for physiological functions in cardiac and nervous systems. We identified two Hcn4 mRNA variants with different transcription start sites and differential expression patterns in mouse brain and heart. Only one mRNA variant was detected in the brain, whereas both variants were found in the heart. Patch clamp recordings of these two variants in HEK293H cells revealed different electrophysiological properties in channel activation. Mutagenesis studies showed that three positively charged amino acids (Arg-9, Lys-10, and Lys-22) contribute to the functional difference. Our results demonstrate that HCN4 channels are expressed in different patterns in mouse brain and heart and that the N terminus is important for HCN4 channel activation.
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