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- Publisher Website: 10.1113/jphysiol.2003.039768
- Scopus: eid_2-s2.0-0037336635
- PMID: 12562911
- WOS: WOS:000183570500002
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Article: Molecular basis of the effect of potassium on heterologously expressed pacemaker (HCN) channels
Title | Molecular basis of the effect of potassium on heterologously expressed pacemaker (HCN) channels |
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Authors | |
Keywords | Chemicals And Cas Registry Numbers |
Issue Date | 2003 |
Publisher | Wiley-Blackwell Publishing Ltd.. The Journal's web site is located at http://www.wiley.com/bw/journal.asp?ref=0022-3751 |
Citation | Journal Of Physiology, 2003, v. 547 n. 2, p. 349-356 How to Cite? |
Abstract | Hyperpolarization-activated cyclic-nucleotide-gated (HCN) channels modulate the firing rates of neuronal and cardiac pacemaker cells. HCN channels resemble voltage-gated K+ channels structurally, but much less is known about their structure-function correlation. Although modulation of K+ channel gating by external K+ is a well-known phenomenon, such a link has not been established for HCN channels. Here we examined the effects of external permeant (K+, Na+ and Li+) and non-permeant (NMG+) ions on HCN1 and HCN2 gating. Substituting 64 of 96 mM external K+ with Na+, Li+ or NMG+ positively shifted steady-state activation (∼13 mV), and preferentially slowed activation of HCN1. Mutating the pore variant C-terminal to the GYG motif in HCN1, A352, to the analogous conserved Asp in K+ channels or Arg in HCN2 produced a significant hyperpolarizing activation shift (by 5-15 mV), slowed gating kinetics (up to 6-fold), and abolished or attenuated gating responses to external K+. Whereas Na+, Li+ and NMG+ substitutions produced depolarizing activation shifts of HCN2 similar to those of HCN1, deactivation but not activation of HCN2 was exclusively decelerated. We conclude that gating and permeation of HCN channels are coupled, and that modulation of this 'pore-to-gate' coupling by external K+ is isoform-specific. |
Persistent Identifier | http://hdl.handle.net/10722/91543 |
ISSN | 2023 Impact Factor: 4.7 2023 SCImago Journal Rankings: 1.708 |
PubMed Central ID | |
ISI Accession Number ID | |
References |
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Azene, EM | en_HK |
dc.contributor.author | Xue, T | en_HK |
dc.contributor.author | Li, RA | en_HK |
dc.date.accessioned | 2010-09-17T10:21:06Z | - |
dc.date.available | 2010-09-17T10:21:06Z | - |
dc.date.issued | 2003 | en_HK |
dc.identifier.citation | Journal Of Physiology, 2003, v. 547 n. 2, p. 349-356 | en_HK |
dc.identifier.issn | 0022-3751 | en_HK |
dc.identifier.uri | http://hdl.handle.net/10722/91543 | - |
dc.description.abstract | Hyperpolarization-activated cyclic-nucleotide-gated (HCN) channels modulate the firing rates of neuronal and cardiac pacemaker cells. HCN channels resemble voltage-gated K+ channels structurally, but much less is known about their structure-function correlation. Although modulation of K+ channel gating by external K+ is a well-known phenomenon, such a link has not been established for HCN channels. Here we examined the effects of external permeant (K+, Na+ and Li+) and non-permeant (NMG+) ions on HCN1 and HCN2 gating. Substituting 64 of 96 mM external K+ with Na+, Li+ or NMG+ positively shifted steady-state activation (∼13 mV), and preferentially slowed activation of HCN1. Mutating the pore variant C-terminal to the GYG motif in HCN1, A352, to the analogous conserved Asp in K+ channels or Arg in HCN2 produced a significant hyperpolarizing activation shift (by 5-15 mV), slowed gating kinetics (up to 6-fold), and abolished or attenuated gating responses to external K+. Whereas Na+, Li+ and NMG+ substitutions produced depolarizing activation shifts of HCN2 similar to those of HCN1, deactivation but not activation of HCN2 was exclusively decelerated. We conclude that gating and permeation of HCN channels are coupled, and that modulation of this 'pore-to-gate' coupling by external K+ is isoform-specific. | en_HK |
dc.language | eng | en_HK |
dc.publisher | Wiley-Blackwell Publishing Ltd.. The Journal's web site is located at http://www.wiley.com/bw/journal.asp?ref=0022-3751 | en_HK |
dc.relation.ispartof | Journal of Physiology | en_HK |
dc.subject | Chemicals And Cas Registry Numbers | en_HK |
dc.title | Molecular basis of the effect of potassium on heterologously expressed pacemaker (HCN) channels | en_HK |
dc.type | Article | en_HK |
dc.identifier.email | Li, RA:ronaldli@hkucc.hku.hk | en_HK |
dc.identifier.authority | Li, RA=rp01352 | en_HK |
dc.description.nature | link_to_subscribed_fulltext | - |
dc.identifier.doi | 10.1113/jphysiol.2003.039768 | en_HK |
dc.identifier.pmid | 12562911 | - |
dc.identifier.pmcid | PMC2342664 | - |
dc.identifier.scopus | eid_2-s2.0-0037336635 | en_HK |
dc.relation.references | http://www.scopus.com/mlt/select.url?eid=2-s2.0-0037336635&selection=ref&src=s&origin=recordpage | en_HK |
dc.identifier.volume | 547 | en_HK |
dc.identifier.issue | 2 | en_HK |
dc.identifier.spage | 349 | en_HK |
dc.identifier.epage | 356 | en_HK |
dc.identifier.isi | WOS:000183570500002 | - |
dc.publisher.place | United Kingdom | en_HK |
dc.identifier.scopusauthorid | Azene, EM=6602472909 | en_HK |
dc.identifier.scopusauthorid | Xue, T=7005064190 | en_HK |
dc.identifier.scopusauthorid | Li, RA=7404724466 | en_HK |
dc.identifier.citeulike | 9713368 | - |
dc.identifier.issnl | 0022-3751 | - |