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Article: Pore-to-gate coupling of HCN channels revealed by a pore variant that contributes to gating but not permeation

TitlePore-to-gate coupling of HCN channels revealed by a pore variant that contributes to gating but not permeation
Authors
KeywordsChemicals and CAS registry numbers
Issue Date2005
PublisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/wps/find/journaldescription.cws_home/622790/description
Citation
Biochemical and Biophysical Research Communications, 2005, v. 327 n. 4, p. 1131-1142 How to Cite?
AbstractAlthough ample evidence suggests the presence of an intracellular activation gate in HCN (pacemaker) channels, mutations in the outer pore can alter gating properties. Here we investigated the role of the outer pore residue A354 in HCN1 gating by systematically converting it to the equivalent residues (T, Y, and F) found in K+-channels. A354T negatively shifted steady-state activation (ΔV1/2 ∼ -25 mV), decelerated gating kinetics (by up to 8-fold), and abolished the effects of external ions on gating. A354Y and A354F did not yield functional currents when expressed alone, although immunofluorescence microscopy indicated the presence of these channel proteins on the membrane surface. Currents recorded after co-expressing A354Y with WT HCN1 were reduced in amplitude (relative to WT alone) and had changes in gating similar to those of A354T. We conclude that the pore variant at position 354 contributes to gating but not permeation, and that the HCN outer pore may be involved in gating via a pore-to-gate coupling mechanism. © 2004 Elsevier Inc. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/91610
ISSN
2015 Impact Factor: 2.371
2015 SCImago Journal Rankings: 1.152
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorAzene, EMen_HK
dc.contributor.authorSang, Den_HK
dc.contributor.authorTsang, SYen_HK
dc.contributor.authorLi, RAen_HK
dc.date.accessioned2010-09-17T10:22:09Z-
dc.date.available2010-09-17T10:22:09Z-
dc.date.issued2005en_HK
dc.identifier.citationBiochemical and Biophysical Research Communications, 2005, v. 327 n. 4, p. 1131-1142en_HK
dc.identifier.issn0006-291Xen_HK
dc.identifier.urihttp://hdl.handle.net/10722/91610-
dc.description.abstractAlthough ample evidence suggests the presence of an intracellular activation gate in HCN (pacemaker) channels, mutations in the outer pore can alter gating properties. Here we investigated the role of the outer pore residue A354 in HCN1 gating by systematically converting it to the equivalent residues (T, Y, and F) found in K+-channels. A354T negatively shifted steady-state activation (ΔV1/2 ∼ -25 mV), decelerated gating kinetics (by up to 8-fold), and abolished the effects of external ions on gating. A354Y and A354F did not yield functional currents when expressed alone, although immunofluorescence microscopy indicated the presence of these channel proteins on the membrane surface. Currents recorded after co-expressing A354Y with WT HCN1 were reduced in amplitude (relative to WT alone) and had changes in gating similar to those of A354T. We conclude that the pore variant at position 354 contributes to gating but not permeation, and that the HCN outer pore may be involved in gating via a pore-to-gate coupling mechanism. © 2004 Elsevier Inc. All rights reserved.en_HK
dc.languageengen_HK
dc.publisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/wps/find/journaldescription.cws_home/622790/descriptionen_HK
dc.relation.ispartofBiochemical and Biophysical Research Communicationsen_HK
dc.subjectChemicals and CAS registry numbersen_HK
dc.subject.meshAlanine - genetics - metabolismen_HK
dc.subject.meshAmino acid sequenceen_HK
dc.subject.meshAmino acid substitution - geneticsen_HK
dc.subject.meshAnimalsen_HK
dc.subject.meshCell membrane permeabilityen_HK
dc.subject.meshCyclic nucleotide-gated cation channelsen_HK
dc.subject.meshGene expressionen_HK
dc.subject.meshIon channel gating - physiologyen_HK
dc.subject.meshIon channels - chemistry - genetics - metabolismen_HK
dc.subject.meshKineticsen_HK
dc.subject.meshMolecular sequence dataen_HK
dc.subject.meshMutagenesis, site-directeden_HK
dc.subject.meshOocytes - metabolismen_HK
dc.subject.meshPotassium channelsen_HK
dc.subject.meshProtein subunits - chemistry - genetics - metabolismen_HK
dc.subject.meshSequence alignmenten_HK
dc.subject.meshXenopus laevisen_HK
dc.titlePore-to-gate coupling of HCN channels revealed by a pore variant that contributes to gating but not permeationen_HK
dc.typeArticleen_HK
dc.identifier.emailLi, RA:ronaldli@hkucc.hku.hken_HK
dc.identifier.authorityLi, RA=rp01352en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.bbrc.2004.12.127en_HK
dc.identifier.pmid15652514-
dc.identifier.scopuseid_2-s2.0-12344302101en_HK
dc.identifier.hkuros183069-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-12344302101&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume327en_HK
dc.identifier.issue4en_HK
dc.identifier.spage1131en_HK
dc.identifier.epage1142en_HK
dc.identifier.isiWOS:000226667800026-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridAzene, EM=6602472909en_HK
dc.identifier.scopusauthoridSang, D=7004187916en_HK
dc.identifier.scopusauthoridTsang, SY=7102255908en_HK
dc.identifier.scopusauthoridLi, RA=7404724466en_HK

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