ArticleBiophysical journal2002
Pore topology of the hyperpolarization-activated cyclic nucleotide-gated channel from sea urchin sperm.
Article in Biophysical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 16 citations in OpenAlex.
- Article
- Architecture of the HCN selectivity filter and control of cation permeation.Scientific reports · 2012Article
- State-dependent accessibility of the P-S6 linker of pacemaker (HCN) channels supports a dynamic pore-to-gate coupling model.The Journal of membrane biology · 2009Article
- Intracellular Mg2+ is a voltage-dependent pore blocker of HCN channels.American journal of physiology. Cell physiology · 2008Article
- Reversal of HCN channel voltage dependence via bridging of the S4-S5 linker and Post-S6.The Journal of general physiology · 2006Article
- The enhancement of HCN channel instantaneous current facilitated by slow deactivation is regulated by intracellular chloride concentration.Pflugers Archiv : European journal of physiology · 2006Article
- Distinct populations of HCN pacemaker channels produce voltage-dependent and voltage-independent currents.The Journal of general physiology · 2006Article
- A homology model of the pore region of HCN channels.Biophysical journal · 2005Article
- Evolving potassium channels by means of yeast selection reveals structural elements important for selectivity.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The current flow through hyperpolarization-activated cyclic nucleotide-gated (HCN) channels, referred to as I(h), plays a major role in several fundamental biological processes. The sequence of the presumed pore region of HCN channels is reminiscent of that of most known K(+)-selective channels. In the present work, the pore topology of an HCN channel from sea urchin sperm, called SpHCN, was investigated by means of the substituted-cysteine accessibility method (SCAM). The I(h) current in the wild-type (w.t.) SpHCN channel was irreversibly blocked by intracellular Cd(2+). This blockage was not observed in mutant C428S. Extracellular Cd(2+) did not cause any inhibition of the I(h) current in the w.t. SpHCN channel, but blocked the current in mutant channels K433C and F434C. Large extracellular anions blocked the current both in the w.t. and K433Q mutant channel. These results suggest that 1) cysteine in position 428 faces the intracellular medium; 2) lysine and phenylalanine in position 433 and 434, respectively, face the extracellular side of the membrane; and 3) lysine 433 does not mediate the anion blockade. Additionally, our study confirms that the K(+) channel signature sequence GYG also forms the inner pore in HCN channels.
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