Calmodulin Interaction with hEAG1 Visualized by FRET Microscopy 英文参考文献.docVIP

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Calmodulin Interaction with hEAG1 Visualized by FRET Microscopy 英文参考文献.doc

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Calmodulin Interaction with hEAG1 Visualized by FRET Microscopy 英文参考文献

CalmodulinInteractionwithhEAG1VisualizedbyFRET Microscopy J.TiagoGonc?alves1*¤,WalterStu¨hmer1,2 1MolecularBiologyofNeuronalSignals,Max-PlanckInstitute forExperimentalMedicine,Go¨ttingen,Germany,2DFGResearchCenterforMolecularPhysiologyofthe Brain,Go¨ttingen,Germany Abstract Background: Ca2+-mediated regulation of ion channels provides a link between intracellular signaling pathways and membrane electrical activity. Intracellular Ca inhibits the voltage-gated potassium channel EAG1 through the direct 2+ bindingofcalmodulin(CaM).ThreeCaMbindingsites(BD-C1:674-683,BD-C2:711-721,BD-N:151-165)havebeenidentified inapeptidescreenandwereproposedtomediatebinding.TheparticipationofthethreesitesinCaMbindingtothenative channel,however,remainsunclear. Methodology/Principal Findings: Here we studied the binding of Ca2+/CaM to the EAG channel by visualizing the interactionbetweenYFP-labeledCaMandCerulean-labeledhEAG1inmammaliancellsbyFRET.Theresultsofourcellular approachsubstantiatethattwoCaMbindingsitesarepredominantlyinvolved;thehigh-affinity1-8-14basedCaMbinding domainintheN-terminusandthesecondC-terminalbindingdomainBD-C2.Mutationsatthesesitescompletelyabolished CaMbindingtohEAG1. Conclusions/Significance:WedemonstratedthattheBD-NandBD-C2bindingdomainsaresufficientforCaMbindingto thenativechannel,and,therefore,thatBD-C1isunabletobindCaMindependently. Citation: Gonc?alves JT, Stu¨hmer W (2010) Calmodulin Interaction with hEAG1 Visualized by FRET Microscopy. PLoS ONE 5(5): e10873. doi:10.1371/ journal.pone.0010873 Editor:RichardSteinhardt,UniversityofCalifornia,UnitedStatesofAmerica ReceivedJanuary8,2010;AcceptedMay4,2010;PublishedMay27,2010 Copyright:?2010Gonc?alves,Stu¨hmer.Thisisanopen-accessarticledistributedunderthetermsoftheCreativeCommonsAttributionLicense,whichpermits unrestricteduse,distribution,andreproductioninanymedium,providedtheoriginalauthorandsourcearecredited. Funding:ThisworkwassupportedbytheDeutscheForschungsgemeinschaft(www.dfg.de)throughthefollowingfund