Non-Native R1 Substitution in the S4 Domain Uniquely Alters Kv4.3 Channel Gating 英文参考文献.docVIP
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Non-Native R1 Substitution in the S4 Domain Uniquely Alters Kv4.3 Channel Gating 英文参考文献
Non-NativeR1SubstitutionintheS4DomainUniquely
AltersKv4.3ChannelGating
MatthewR.Skerritt,DonaldL.Campbell*
DepartmentofPhysiologyBiophysics,SchoolofMedicineandBiomedicalSciences,UniversityatBuffalo,StateUniversityofNewYork,Buffalo,NewYork,UnitedStates
ofAmerica
Abstract
TheS4transmembranedomaininShaker(Kv1)voltage-sensitivepotassiumchannelshasfourbasicresidues(R1–R4)that
areresponsibleforcarryingthemajorityofgatingcharge.InKv4channels,however,R1isreplacedbyaneutralvalineat
position 287. Among other differences, Kv4 channels display prominent closed state inactivation, a mechanism which is
minimalinShaker.TodetermineiftheabsenceofR1isresponsibleforimportantvariationingatingcharacteristicsbetween
thetwochanneltypes,weintroducedtheV287RmutantintoKv4.3andanalyzeditseffectsonseveralvoltagesensitive
gating transitions. We found that the mutant increased the voltage sensitivity of steady-state activation and altered the
kineticsofactivationanddeactivationprocesses.Althoughthekineticsofmacroscopicinactivationwereminimallyaffected,
the characteristics of closed-state inactivation and recovery from open and closed inactivated states were significantly
altered.TheabsenceofR1canonlypartiallyaccountfordifferencesintheeffectivevoltagesensitivityofgatingbetween
ShakerandKv4.3.TheseresultssuggestthattheS4domainservesanimportantfunctionalroleinKv4channelactivation
anddeactivationprocesses,andalsothoseofclosed-stateinactivationandrecovery.
Citation: Skerritt MR, Campbell DL (2008) Non-Native R1 Substitution in the S4 Domain Uniquely Alters Kv4.3 Channel Gating. PLoS ONE 3(11): e3773.
doi:10.1371/journal.pone.0003773
Editor:ArnoldSchwartz,UniversityofCincinnati,UnitedStatesofAmerica
ReceivedSeptember30,2008;AcceptedNovember1,2008;PublishedNovember20,2008
Copyright:?2008Skerritt,Campbell.Thisisanopen-accessarticledistributedunderthetermsoftheCreativeCommonsAttributionLicense,whichpermits
unrestricteduse,distribution,andreproductioninanymedium,providedtheoriginalauthorandsourcearecred
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