A Skeletal Muscle Ryanodine Receptor Interaction Domain in Triadin 英文参考文献.docVIP

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A Skeletal Muscle Ryanodine Receptor Interaction Domain in Triadin 英文参考文献.doc

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A Skeletal Muscle Ryanodine Receptor Interaction Domain in Triadin 英文参考文献

ASkeletalMuscleRyanodineReceptorInteraction DomaininTriadin ElizeWium,AngelaF.Dulhunty,NicoleA.Beard* JohnCurtinSchoolofMedicalResearch,AustralianCapitalTerritory,Australia Abstract Excitation-contractioncouplinginskeletalmuscledepends,inpart,onafunctionalinteractionbetweentheligand-gated ryanodine receptor (RyR1) and integral membrane protein Trisk 95, localized to the sarcoplasmic reticulum membrane. VariousdomainsonTrisk95canassociatewithRyR1,yetthedomainresponsibleforregulatingRyR1activityhasremained elusive.WeexploredthehypothesisthataluminalTrisk95KEKEmotif(residues200–232),knowntopromoteRyR1binding, mayalsoformtheRyR1activationdomain.PeptidescorrespondingtoTrisk95residues200–232or200–231boundtoRyR1 and increased the single channel activity of RyR1 by 1.4960.11-fold and 1.860.15-fold respectively, when added to its luminalside.Asimilarincreasein[3H]ryanodinebinding,whichreflectsopenprobabilityofthechannels,wasalsoobserved. ThisRyR1activationissimilartoactivationinducedbyfulllengthTrisk95.Circulardichroismshowedthatbothpeptides wereintrinsicallydisordered,suggestingadefinedsecondarystructureisnotnecessarytomediateRyR1activation.These dataforthefirsttimedemonstratethatTrisk959s200–231regionisresponsibleforRyR1activation.Furthermore,itshows thatnosecondarystructureisrequiredtoachievethisactivation,theTrisk95residuesthemselvesarecriticalfortheTrisk 95-RyR1interaction. Citation: Wium E, Dulhunty AF, Beard NA (2012) A Skeletal Muscle Ryanodine Receptor Interaction Domain in Triadin. PLoS ONE 7(8): e43817. doi:10.1371/ journal.pone.0043817 Editor:BradleyStevenLaunikonis,UniversityofQueensland,Australia ReceivedMay9,2012;AcceptedJuly26,2012;PublishedAugust24,2012 Copyright: ? 2012 Wium et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricteduse,distribution,andreproductioninanymedium,providedtheoriginalauthorandsourcearecredited. Funding:ThisworkwassupportedbytheAustralianResearchCounci