Erratum: Cyclic dinucleotides bind the C-linker of HCN4 to control channel cAMP responsiveness
نویسندگان
چکیده
منابع مشابه
Cyclic dinucleotides bind the C-linker of HCN4 to control channel cAMP responsiveness.
cAMP mediates autonomic regulation of heart rate by means of hyperpolarization-activated cyclic nucleotide-gated (HCN) channels, which underlie the pacemaker current If. cAMP binding to the C-terminal cyclic nucleotide binding domain enhances HCN open probability through a conformational change that reaches the pore via the C-linker. Using structural and functional analysis, we identified a bin...
متن کاملInvestigating cyclic nucleotide and cyclic dinucleotide binding to HCN channels by surface plasmon resonance
Hyperpolarization-activated cyclic nucleotide-modulated (HCN) channels control cardiac and neuronal rhythmicity. HCN channels contain cyclic nucleotide-binding domain (CNBD) in their C-terminal region linked to the pore-forming transmembrane segment with a C-linker. The C-linker couples the conformational changes caused by the direct binding of cyclic nucleotides to the HCN pore opening. Recent...
متن کاملThe HCN4 channel mutation D553N associated with bradycardia has a C-linker mediated gating defect.
BACKGROUND/AIMS The D553N mutation located in the C-linker of the cardiac pacemaker channel HCN4 is thought to cause sino-atrial dysfunction via a pronounced dominant-negative trafficking defect. Since HCN4 mutations usually have a minor defect in channel gating, it was our aim to further characterize the disease causing mechanism of D553N. METHODS Fluorescence microscopy, FACS, TEVC and patc...
متن کاملC-Linker of Cyclic Nucleotide–gated Channels Controls Coupling of Ligand Binding to Channel Gating
Cyclic nucleotide-gated channels are composed of a core transmembrane domain, structurally homologous to the voltage-gated K+ channels, and a cytoplasmic ligand-binding domain. These two modules are joined by approximately 90 conserved amino acids, the C-linker, whose precise role in the mechanism of channel activation by cyclic nucleotides is poorly understood. We examined cyclic nucleotide-ga...
متن کاملCellular context and multiple channel domains determine cAMP sensitivity of HCN4 channels: Ligand-independent relief of autoinhibition in HCN4
Hyperpolarization-activated, cyclic nucleotide-sensitive (HCN) channels produce the I(f) and I(h) currents, which are critical for cardiac pacemaking and neuronal excitability, respectively. HCN channels are modulated by cyclic AMP (cAMP), which binds to a conserved cyclic nucleotide-binding domain (CNBD) in the C terminus. The unliganded CNBD has been shown to inhibit voltage-dependent gating ...
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ژورنال
عنوان ژورنال: Nature Chemical Biology
سال: 2014
ISSN: 1552-4450,1552-4469
DOI: 10.1038/nchembio0814-692b